Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

2SRT

CATALYTIC DOMAIN OF HUMAN STROMELYSIN-1 AT PH 5.5 AND 40OC COMPLEXED WITH INHIBITOR

Replaces:  1SRT
Functional Information from GO Data
ChainGOidnamespacecontents
A0004222molecular_functionmetalloendopeptidase activity
A0006508biological_processproteolysis
A0008237molecular_functionmetallopeptidase activity
A0008270molecular_functionzinc ion binding
A0031012cellular_componentextracellular matrix
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 257
ChainResidue
AHIS201
AHIS205
AHIS211
A8MI256

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 258
ChainResidue
AHIS151
ATYR155
AHIS166
AHIS179

site_idAC3
Number of Residues11
DetailsBINDING SITE FOR RESIDUE 8MI A 256
ChainResidue
AASN162
ALEU164
AALA165
ALEU197
AHIS201
AHIS211
ALEU218
ATYR220
ALEU222
ATYR223
AZN257

site_idS1
Number of Residues8
Details
ChainResidue
ALEU164
ALEU197
AVAL198
AHIS201
ALEU218
ATYR220
ALEU222
ATYR223

site_idS2
Number of Residues1
Details
ChainResidue
AASP183

site_idS3
Number of Residues3
Details
ChainResidue
AASN162
ALEU164
ATYR223

Functional Information from PROSITE/UniProt
site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. VAAHEIGHSL
ChainResidueDetails
AVAL198-LEU207

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues16
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"8740360","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1hfs
ChainResidueDetails
AMET219
AGLU202

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1hfs
ChainResidueDetails
AGLU202

site_idMCSA1
Number of Residues4
DetailsM-CSA 591
ChainResidueDetails
AHIS201metal ligand
AGLU202proton acceptor, proton donor
AHIS205metal ligand
AHIS211metal ligand

239149

数据于2025-07-23公开中

PDB statisticsPDBj update infoContact PDBjnumon