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4AR8

Crystal structure of the peptidase domain of collagenase T from Clostridium tetani complexed with the peptidic inhibitor isoamyl- phosphonyl-Gly-Pro-Ala at 2.05 angstrom resolution.

Functional Information from GO Data
ChainGOidnamespacecontents
A0004222molecular_functionmetalloendopeptidase activity
A0005576cellular_componentextracellular region
A0006508biological_processproteolysis
A0008270molecular_functionzinc ion binding
B0004222molecular_functionmetalloendopeptidase activity
B0005576cellular_componentextracellular region
B0006508biological_processproteolysis
B0008270molecular_functionzinc ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 1731
ChainResidue
AHIS465
AHIS469
AGLU499
CIP80

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 1732
ChainResidue
AHOH2055
AGLU440
AGLY473
AILE477
AGLY479
AHOH2036

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 1731
ChainResidue
BHIS465
BHIS469
BGLU499
DIP80

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 1732
ChainResidue
BGLU440
BGLY473
BILE477
BGLY479
BHOH2027
BHOH2045

site_idAC5
Number of Residues16
DetailsBINDING SITE FOR CHAIN C OF ISOAMYL-PHOSPHONYL-GLY-PRO-ALA
ChainResidue
AGLY435
AGLY436
ASER455
ATYR457
ALEU462
AHIS465
AGLU466
AHIS469
AGLU499
AGLU503
ATRP545
ATYR548
AZN1731
AHOH2050
AHOH2051
AHOH2056

site_idAC6
Number of Residues17
DetailsBINDING SITE FOR CHAIN D OF ISOAMYL-PHOSPHONYL-GLY-PRO-ALA
ChainResidue
BASN434
BGLY435
BGLY436
BILE437
BTYR438
BSER455
BTYR457
BLEU462
BHIS465
BGLU466
BHIS469
BGLU499
BGLU503
BTRP545
BTYR548
BZN1731
BHOH2048

Functional Information from PROSITE/UniProt
site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. LFRHEFTHYL
ChainResidueDetails
ALEU462-LEU471

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10095
ChainResidueDetails
AGLU466
BGLU466

site_idSWS_FT_FI2
Number of Residues10
DetailsBINDING: BINDING => ECO:0000269|PubMed:23703618, ECO:0007744|PDB:4AR8, ECO:0007744|PDB:4AR9
ChainResidueDetails
AILE477
AGLY479
AGLU499
BGLU440
BGLY473
BILE477
BGLY479
BGLU499
AGLU440
AGLY473

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0000269|PubMed:23703618, ECO:0007744|PDB:4AR8, ECO:0007744|PDB:4AR9
ChainResidueDetails
AHIS465
AHIS469
BHIS465
BHIS469

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PDB entries from 2024-06-12

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