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1HTD

STRUCTURAL INTERACTION OF NATURAL AND SYNTHETIC INHIBITORS WITH THE VENOM METALLOPROTEINASE, ATROLYSIN C (HT-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
AHOH479

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 403
ChainResidue
AGLU9
AASP93
ACYS197
AASN200
AHOH416
AHOH430

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 402
ChainResidue
BHIS142
BHIS146
BHIS152
BHOH302

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 404
ChainResidue
BGLU9
BASP93
BCYS197
BASN200
BHOH349
BHOH357

site_idCAA
Number of Residues3
DetailsCALCIUM ION BINDING SITE IN CHAIN A
ChainResidue
AGLU9
AASP93
AASN200

site_idCAB
Number of Residues3
DetailsCALCIUM ION BINDING SITE IN CHAIN B
ChainResidue
BGLU9
BASP93
BASN200

site_idZNA
Number of Residues3
DetailsZINC BINDING SITE IN CHAIN A. THEY ARE IDENTIFIED BY CONSERVED RESIDUES HEXXHXXGXXH IN BOTH VENOM AND MAMMALIAN COLLAGENASES
ChainResidue
AHIS142
AHIS146
AHIS152

site_idZNB
Number of Residues3
DetailsZINC BINDING SITE IN CHAIN B. THEY ARE IDENTIFIED BY CONSERVED RESIDUES HEXXHXXGXXH IN BOTH VENOM AND MAMMALIAN COLLAGENASES
ChainResidue
BHIS142
BHIS146
BHIS152

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

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PDB entries from 2024-07-17

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