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1ATL

Structural interaction of natural and synthetic inhibitors with the VENOM METALLOPROTEINASE, ATROLYSIN C (FORM-D)

Functional Information from GO Data
ChainGOidnamespacecontents
A0004222molecular_functionmetalloendopeptidase activity
A0006508biological_processproteolysis
A0008237molecular_functionmetallopeptidase activity
B0004222molecular_functionmetalloendopeptidase activity
B0006508biological_processproteolysis
B0008237molecular_functionmetallopeptidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 401
ChainResidue
AHIS142
AHIS146
AHIS152
A0QI301

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 403
ChainResidue
AGLU9
AASP93
ACYS197
AASN200
AHOH814

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 402
ChainResidue
BHIS142
BHIS146
BHIS152
B0QI311

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 404
ChainResidue
BGLU9
BASP93
BCYS197
BASN200
BHOH834
BHOH921

site_idAC5
Number of Residues14
DetailsBINDING SITE FOR RESIDUE 0QI A 301
ChainResidue
AGLU106
ATHR107
ALEU108
AGLY109
AHIS142
AGLU143
AHIS146
AHIS152
AILE165
AARG167
APRO168
AGLY169
ALEU170
AZN401

site_idAC6
Number of Residues16
DetailsBINDING SITE FOR RESIDUE 0QI B 311
ChainResidue
BGLU106
BTHR107
BLEU108
BGLY109
BHIS142
BGLU143
BHIS146
BHIS152
BILE165
BARG167
BPRO168
BGLY169
BLEU170
BZN402
BHOH819
BHOH920

Functional Information from PROSITE/UniProt
site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. TMAHELGHNL
ChainResidueDetails
ATHR139-LEU148

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE:
ChainResidueDetails
AGLU143
BGLU143

site_idSWS_FT_FI2
Number of Residues14
DetailsBINDING:
ChainResidueDetails
AGLU9
BHIS142
BHIS146
BHIS152
BCYS197
BASN200
AASP93
AHIS142
AHIS146
AHIS152
ACYS197
AASN200
BGLU9
BASP93

223790

PDB entries from 2024-08-14

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