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2Y6I

Crystal Structure of Collagenase G from Clostridium histolyticum in complex with Isoamylphosphonyl-Gly-Pro-Ala at 3.25 Angstrom Resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0004222molecular_functionmetalloendopeptidase activity
A0005576cellular_componentextracellular region
A0006508biological_processproteolysis
A0008270molecular_functionzinc ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 1791
ChainResidue
AHIS523
AHIS527
AGLU555
AHOH2042
BIPI1

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE FLC A 1793
ChainResidue
AASP737
ASER740
ALYS741
ASER568
ATYR618
AMET622
ATRP736

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE TRS A 1794
ChainResidue
ALYS247
AASN251
ALYS291
APHE295

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE TRS A 1795
ChainResidue
ATHR565
AARG566
ATHR567
ASER568
ALEU675

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE TRS A 1796
ChainResidue
AASP368
AHOH2043

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PEG A 1797
ChainResidue
AALA458
ALEU459
AASN634

site_idAC7
Number of Residues1
DetailsBINDING SITE FOR RESIDUE PEG A 1798
ChainResidue
AGLU619

site_idAC8
Number of Residues7
DetailsBINDING SITE FOR RESIDUE 1PE A 1799
ChainResidue
AALA277
APRO278
AASP279
ATHR284
ATRP337
AASP340
AHOH2044

Functional Information from PROSITE/UniProt
site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. LFRHEYTHYL
ChainResidueDetails
ALEU520-LEU529

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0000305|PubMed:11121400
ChainResidueDetails
AGLU524

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q899Y1, ECO:0000303|PubMed:23703618
ChainResidueDetails
AGLU498
AALA531
AVAL535
AGLY537

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0000269|PubMed:21947205, ECO:0000269|PubMed:23703618, ECO:0007744|PDB:2Y50, ECO:0007744|PDB:2Y6I, ECO:0007744|PDB:4ARE
ChainResidueDetails
AHIS523
AHIS527

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:21947205, ECO:0000269|PubMed:23703618, ECO:0007744|PDB:2Y50, ECO:0007744|PDB:2Y6I, ECO:0007744|PDB:4ARE
ChainResidueDetails
AGLU555

site_idSWS_FT_FI5
Number of Residues5
DetailsBINDING: BINDING => ECO:0000269|PubMed:23703618, ECO:0007744|PDB:4AQO
ChainResidueDetails
AASN795
ALYS796
AASP823
AASP825
AASP864

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PDB entries from 2024-10-16

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