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1SLM

CRYSTAL STRUCTURE OF FIBROBLAST STROMELYSIN-1: THE C-TRUNCATED HUMAN PROENZYME

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
ACYS75
AHIS201
AHIS205
AHIS211

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 258
ChainResidue
AHIS151
AASP153
AHIS166
ATYR168
AHIS179

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 259
ChainResidue
AASP158
AGLY159
AGLY161
AVAL163
AASP181
AGLU184

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 260
ChainResidue
AASP141
AGLY173
AASN175
AASP177
AHOH306
AHOH312

site_idCA1
Number of Residues6
DetailsCA1 ARE THE LIGANDS OF THE CALCIUM ION CA 259
ChainResidue
AGLY159
AGLY161
AVAL163
AASP181
AGLU184
AASP158

site_idCA2
Number of Residues6
DetailsCA2 ARE THE LIGANDS OF THE CALCIUM ION CA 260
ChainResidue
AASP141
AGLY173
AASN175
AASP177
AHOH306
AHOH312

site_idZN1
Number of Residues4
DetailsZN1 ARE THE LIGANDS OF THE CATALYTIC (ZN 257) ZINC ION.
ChainResidue
ACYS75
AHIS201
AHIS205
AHIS211

site_idZN2
Number of Residues4
DetailsZN2 ARE THE LIGANDS OF THE STRUCTURAL (ZN 258) ZINC ION.
ChainResidue
AHIS151
AASP153
AHIS166
AHIS179

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

site_idPS00546
Number of Residues8
DetailsCYSTEINE_SWITCH Matrixins cysteine switch. PRCGvPDV
ChainResidueDetails
APRO73-VAL80

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE:
ChainResidueDetails
AGLU202

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: in inhibited form
ChainResidueDetails
ACYS75

site_idSWS_FT_FI3
Number of Residues16
DetailsBINDING:
ChainResidueDetails
AASP107
AGLY173
AASN175
AASP177
AHIS179
AASP181
AASP182
AGLU184
AASP141
AHIS151
AASP153
AASP158
AGLY159
AGLY161
AVAL163
AHIS166

site_idSWS_FT_FI4
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:8740360
ChainResidueDetails
AHIS201
AHIS205
AHIS211

Catalytic Information from CSA
site_idCSA1
Number of Residues1
Details
ChainResidueDetails
AGLU202

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

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PDB entries from 2024-05-01

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