ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Chymotrypsin-like elastase family member 1

Intermolecular
Cysteine 240 and cysteine 29 of Chymotrypsin/elastase isoinhibitor 1
Cysteine 210 and cysteine 14 of Chymotrypsin/elastase isoinhibitor 1
Cysteine 72 and cysteine 109 of Elafin
Cysteine 72 and cysteine 83 of Elafin
Cysteine 240 and cysteine 14 of Chymotrypsin/elastase isoinhibitor 1
Cysteine 56 and cysteine 109 of Elafin
Cysteine 72 and cysteine 12 of PI-stichotoxin-She2a
Cysteine 56 and cysteine 83 of Elafin
Cysteine 210 and cysteine 33 of Chymotrypsin/elastase isoinhibitor 1 L
Cysteine 56 and cysteine 33 of Chymotrypsin/elastase isoinhibitor 1 L
More...
Cysteine 240 and cysteine 33 of Chymotrypsin/elastase isoinhibitor 1 L
Cysteine 56 and cysteine 12 of PI-stichotoxin-She2a
Cysteine 210 and cysteine 29 of Chymotrypsin/elastase isoinhibitor 1
Cysteine 240 and cysteine 17 of Chymotrypsin/elastase isoinhibitor 1
Intramolecular
Cysteine 153 and cysteine 220
Cysteine 210 and cysteine 240
Cysteine 184 and cysteine 200
Cysteine 56 and cysteine 72
A redox-regulated disulphide may form between cysteine 240 of Chymotrypsin-like elastase family member 1 and cysteine 29 of Chymotrypsin/elastase isoinhibitor 1 (220 and 29 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
49
PDB code
1eai
Structure name
complex of ascaris chymotrpsin/elastase inhibitor with porcine elastase
Structure deposition date
1999-03-25
Thiol separation (Å)
8
Half-sphere exposure sum ?
80
Minimum pKa ?
nan
% buried
nan
Peptide A name
Chymotrypsin-like elastase family member 1
Peptide B name
Chymotrypsin/elastase isoinhibitor 1
Peptide A accession
P00772
Peptide B accession
P07851
Peptide A residue number
240
Peptide B residue number
29

Ligandability

Cysteine 240 of Chymotrypsin-like elastase family member 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 29 of Chymotrypsin/elastase isoinhibitor 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form between cysteine 210 of Chymotrypsin-like elastase family member 1 and cysteine 14 of Chymotrypsin/elastase isoinhibitor 1 (191 and 14 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
1eai
Structure name
complex of ascaris chymotrpsin/elastase inhibitor with porcine elastase
Structure deposition date
1999-03-25
Thiol separation (Å)
8
Half-sphere exposure sum ?
83
Minimum pKa ?
nan
% buried
nan
Peptide A name
Chymotrypsin-like elastase family member 1
Peptide B name
Chymotrypsin/elastase isoinhibitor 1
Peptide A accession
P00772
Peptide B accession
P07851
Peptide A residue number
210
Peptide B residue number
14

Ligandability

Cysteine 210 of Chymotrypsin-like elastase family member 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 14 of Chymotrypsin/elastase isoinhibitor 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form between cysteine 72 of Chymotrypsin-like elastase family member 1 and cysteine 109 of Elafin (58 and 49 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
1fle
Structure name
crystal structure of elafin complexed with porcine pancreatic elastase
Structure deposition date
1996-07-04
Thiol separation (Å)
8
Half-sphere exposure sum ?
90
Minimum pKa ?
nan
% buried
nan
Peptide A name
Chymotrypsin-like elastase family member 1
Peptide B name
Elafin
Peptide A accession
P00772
Peptide B accession
P19957
Peptide A residue number
72
Peptide B residue number
109

Ligandability

Cysteine 72 of Chymotrypsin-like elastase family member 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 109 of Elafin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form between cysteine 72 of Chymotrypsin-like elastase family member 1 and cysteine 83 of Elafin (58 and 23 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
1fle
Structure name
crystal structure of elafin complexed with porcine pancreatic elastase
Structure deposition date
1996-07-04
Thiol separation (Å)
8
Half-sphere exposure sum ?
98
Minimum pKa ?
nan
% buried
nan
Peptide A name
Chymotrypsin-like elastase family member 1
Peptide B name
Elafin
Peptide A accession
P00772
Peptide B accession
P19957
Peptide A residue number
72
Peptide B residue number
83

Ligandability

Cysteine 72 of Chymotrypsin-like elastase family member 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 83 of Elafin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form between cysteine 240 of Chymotrypsin-like elastase family member 1 and cysteine 14 of Chymotrypsin/elastase isoinhibitor 1 (220 and 14 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
1eai
Structure name
complex of ascaris chymotrpsin/elastase inhibitor with porcine elastase
Structure deposition date
1999-03-25
Thiol separation (Å)
9
Half-sphere exposure sum ?
76
Minimum pKa ?
nan
% buried
nan
Peptide A name
Chymotrypsin-like elastase family member 1
Peptide B name
Chymotrypsin/elastase isoinhibitor 1
Peptide A accession
P00772
Peptide B accession
P07851
Peptide A residue number
240
Peptide B residue number
14

Ligandability

Cysteine 240 of Chymotrypsin-like elastase family member 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 14 of Chymotrypsin/elastase isoinhibitor 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form between cysteine 56 of Chymotrypsin-like elastase family member 1 and cysteine 109 of Elafin (42 and 49 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
1fle
Structure name
crystal structure of elafin complexed with porcine pancreatic elastase
Structure deposition date
1996-07-04
Thiol separation (Å)
8
Half-sphere exposure sum ?
88
Minimum pKa ?
nan
% buried
nan
Peptide A name
Chymotrypsin-like elastase family member 1
Peptide B name
Elafin
Peptide A accession
P00772
Peptide B accession
P19957
Peptide A residue number
56
Peptide B residue number
109

Ligandability

Cysteine 56 of Chymotrypsin-like elastase family member 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 109 of Elafin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form between cysteine 72 of Chymotrypsin-like elastase family member 1 and cysteine 12 of PI-stichotoxin-She2a. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
3uou
Structure name
crystal structure of the kunitz-type protease inhibitor shpi-1 lys13leu mutant in complex with pancreatic elastase
Structure deposition date
2011-11-17
Thiol separation (Å)
8
Half-sphere exposure sum ?
102
Minimum pKa ?
nan
% buried
nan
Peptide A name
Chymotrypsin-like elastase family member 1
Peptide B name
PI-stichotoxin-She2a
Peptide A accession
P00772
Peptide B accession
P31713
Peptide A residue number
72
Peptide B residue number
12

Ligandability

Cysteine 72 of Chymotrypsin-like elastase family member 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 12 of PI-stichotoxin-She2a

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form between cysteine 56 of Chymotrypsin-like elastase family member 1 and cysteine 83 of Elafin (42 and 23 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
1fle
Structure name
crystal structure of elafin complexed with porcine pancreatic elastase
Structure deposition date
1996-07-04
Thiol separation (Å)
8
Half-sphere exposure sum ?
96
Minimum pKa ?
nan
% buried
nan
Peptide A name
Chymotrypsin-like elastase family member 1
Peptide B name
Elafin
Peptide A accession
P00772
Peptide B accession
P19957
Peptide A residue number
56
Peptide B residue number
83

Ligandability

Cysteine 56 of Chymotrypsin-like elastase family member 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 83 of Elafin

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form between cysteine 210 of Chymotrypsin-like elastase family member 1 and cysteine 33 of Chymotrypsin/elastase isoinhibitor 1 (191 and 33 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
1eai
Structure name
complex of ascaris chymotrpsin/elastase inhibitor with porcine elastase
Structure deposition date
1999-03-25
Thiol separation (Å)
9
Half-sphere exposure sum ?
85
Minimum pKa ?
nan
% buried
nan
Peptide A name
Chymotrypsin-like elastase family member 1
Peptide B name
Chymotrypsin/elastase isoinhibitor 1
Peptide A accession
P00772
Peptide B accession
P07851
Peptide A residue number
210
Peptide B residue number
33

Ligandability

Cysteine 210 of Chymotrypsin-like elastase family member 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 33 of Chymotrypsin/elastase isoinhibitor 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form between cysteine 56 of Chymotrypsin-like elastase family member 1 and cysteine 33 of Chymotrypsin/elastase isoinhibitor 1 (42 and 33 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
1eai
Structure name
complex of ascaris chymotrpsin/elastase inhibitor with porcine elastase
Structure deposition date
1999-03-25
Thiol separation (Å)
9
Half-sphere exposure sum ?
78
Minimum pKa ?
nan
% buried
nan
Peptide A name
Chymotrypsin-like elastase family member 1
Peptide B name
Chymotrypsin/elastase isoinhibitor 1
Peptide A accession
P00772
Peptide B accession
P07851
Peptide A residue number
56
Peptide B residue number
33

Ligandability

Cysteine 56 of Chymotrypsin-like elastase family member 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 33 of Chymotrypsin/elastase isoinhibitor 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form between cysteine 240 of Chymotrypsin-like elastase family member 1 and cysteine 33 of Chymotrypsin/elastase isoinhibitor 1 (220 and 33 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
1eai
Structure name
complex of ascaris chymotrpsin/elastase inhibitor with porcine elastase
Structure deposition date
1999-03-25
Thiol separation (Å)
10
Half-sphere exposure sum ?
78
Minimum pKa ?
nan
% buried
nan
Peptide A name
Chymotrypsin-like elastase family member 1
Peptide B name
Chymotrypsin/elastase isoinhibitor 1
Peptide A accession
P00772
Peptide B accession
P07851
Peptide A residue number
240
Peptide B residue number
33

Ligandability

Cysteine 240 of Chymotrypsin-like elastase family member 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 33 of Chymotrypsin/elastase isoinhibitor 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form between cysteine 56 of Chymotrypsin-like elastase family member 1 and cysteine 12 of PI-stichotoxin-She2a. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
38
PDB code
3uou
Structure name
crystal structure of the kunitz-type protease inhibitor shpi-1 lys13leu mutant in complex with pancreatic elastase
Structure deposition date
2011-11-17
Thiol separation (Å)
9
Half-sphere exposure sum ?
100
Minimum pKa ?
nan
% buried
nan
Peptide A name
Chymotrypsin-like elastase family member 1
Peptide B name
PI-stichotoxin-She2a
Peptide A accession
P00772
Peptide B accession
P31713
Peptide A residue number
56
Peptide B residue number
12

Ligandability

Cysteine 56 of Chymotrypsin-like elastase family member 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 12 of PI-stichotoxin-She2a

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form between cysteine 210 of Chymotrypsin-like elastase family member 1 and cysteine 29 of Chymotrypsin/elastase isoinhibitor 1 (191 and 29 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
37
PDB code
1eai
Structure name
complex of ascaris chymotrpsin/elastase inhibitor with porcine elastase
Structure deposition date
1999-03-25
Thiol separation (Å)
9
Half-sphere exposure sum ?
87
Minimum pKa ?
nan
% buried
nan
Peptide A name
Chymotrypsin-like elastase family member 1
Peptide B name
Chymotrypsin/elastase isoinhibitor 1
Peptide A accession
P00772
Peptide B accession
P07851
Peptide A residue number
210
Peptide B residue number
29

Ligandability

Cysteine 210 of Chymotrypsin-like elastase family member 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 29 of Chymotrypsin/elastase isoinhibitor 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form between cysteine 240 of Chymotrypsin-like elastase family member 1 and cysteine 17 of Chymotrypsin/elastase isoinhibitor 1 (220 and 17 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
37
PDB code
1eai
Structure name
complex of ascaris chymotrpsin/elastase inhibitor with porcine elastase
Structure deposition date
1999-03-25
Thiol separation (Å)
9
Half-sphere exposure sum ?
80
Minimum pKa ?
nan
% buried
nan
Peptide A name
Chymotrypsin-like elastase family member 1
Peptide B name
Chymotrypsin/elastase isoinhibitor 1
Peptide A accession
P00772
Peptide B accession
P07851
Peptide A residue number
240
Peptide B residue number
17

Ligandability

Cysteine 240 of Chymotrypsin-like elastase family member 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 17 of Chymotrypsin/elastase isoinhibitor 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Chymotrypsin-like elastase family member 1 between cysteines 153 and 220 (136 and 201 respectively in this structure).

Details

Redox score ?
79
PDB code
2est
Structure name
crystallographic study of the binding of a trifluoroacetyl dipeptide anilide inhibitor with elastase
Structure deposition date
1986-03-24
Thiol separation (Å)
3
Half-sphere exposure sum ?
73
Minimum pKa ?
8
% buried
77
Peptide accession
P00772
Residue number A
153
Residue number B
220
Peptide name
Chymotrypsin-like elastase family member 1

Ligandability

Cysteine 153 of Chymotrypsin-like elastase family member 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 220 of Chymotrypsin-like elastase family member 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Chymotrypsin-like elastase family member 1 between cysteines 210 and 240 (191 and 220 respectively in this structure).

Details

Redox score ?
78
PDB code
2est
Structure name
crystallographic study of the binding of a trifluoroacetyl dipeptide anilide inhibitor with elastase
Structure deposition date
1986-03-24
Thiol separation (Å)
3
Half-sphere exposure sum ?
86
Minimum pKa ?
7
% buried
58
Peptide accession
P00772
Residue number A
210
Residue number B
240
Peptide name
Chymotrypsin-like elastase family member 1

Ligandability

Cysteine 210 of Chymotrypsin-like elastase family member 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 240 of Chymotrypsin-like elastase family member 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Chymotrypsin-like elastase family member 1 between cysteines 184 and 200 (168 and 182 respectively in this structure).

Details

Redox score ?
73
PDB code
3moc
Structure name
investigation of global and local effects of radiation damage on porcine pancreatic elastase
Structure deposition date
2010-04-22
Thiol separation (Å)
3
Half-sphere exposure sum ?
83
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00772
Residue number A
184
Residue number B
200
Peptide name
Chymotrypsin-like elastase family member 1

Ligandability

Cysteine 184 of Chymotrypsin-like elastase family member 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 200 of Chymotrypsin-like elastase family member 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Chymotrypsin-like elastase family member 1 between cysteines 56 and 72 (42 and 58 respectively in this structure).

Details

Redox score ?
73
PDB code
3mu1
Structure name
comparison of the character and the speed of x-ray-induced structural changes of porcine pancreatic elastase at two temperatures, 100 and 15k
Structure deposition date
2010-05-01
Thiol separation (Å)
3
Half-sphere exposure sum ?
84
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00772
Residue number A
56
Residue number B
72
Peptide name
Chymotrypsin-like elastase family member 1

Ligandability

Cysteine 56 of Chymotrypsin-like elastase family member 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 72 of Chymotrypsin-like elastase family member 1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

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