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1SLN

CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN FIBROBLAST STROMELYSIN-1 INHIBITED WITH THE N-CARBOXY-ALKYL INHIBITOR L-702,842

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
AASP153
AHIS166
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_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CA A 261
ChainResidue
AASP107
AASP182
AGLU184

site_idAC6
Number of Residues22
DetailsBINDING SITE FOR RESIDUE 8MI A 256
ChainResidue
AGLY152
AASP153
APHE154
AASN162
ALEU164
AALA165
ALEU197
AVAL198
AHIS201
AGLU202
AHIS205
AHIS211
ALEU218
ATYR220
APRO221
ALEU222
ATYR223
AZN257
AHOH301
AHOH502
AHOH504
AHOH519

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

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

site_idCA3
Number of Residues3
DetailsCA3 ARE THE LIGANDS OF THE CALCIUM ION CA 261
ChainResidue
AASP107
AASP182
AGLU184

site_idINH
Number of Residues18
DetailsSITE INH IS THE BINDING SITE FOR THE N-CARBOXY-ALKYL INHIBITOR L-702,842, DENOTED INH 256.
ChainResidue
AASN162
AHIS211
ALEU218
ATYR220
APRO221
ALEU222
ATYR223
AZN257
AHOH301
AHOH502
AVAL163
ALEU164
AALA165
ALEU197
AVAL198
AHIS201
AGLU202
AHIS205

site_idZN1
Number of Residues4
DetailsZN1 ARE THE LIGANDS OF THE CATALYTIC (ZN 257) ZINC ION.
ChainResidue
AHIS201
AHIS205
AHIS211
A8MI256

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

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

site_idSWS_FT_FI2
Number of Residues16
DetailsBINDING:
ChainResidueDetails
AASP107
AGLY173
AASN175
AASP177
AHIS179
AASP181
AASP182
AGLU184
AASP141
AHIS151
AASP153
AASP158
AGLY159
AGLY161
AVAL163
AHIS166

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:8740360
ChainResidueDetails
AHIS201
AHIS205
AHIS211

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

223166

PDB entries from 2024-07-31

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