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1USN

CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN FIBROBLAST STROMELYSIN-1 INHIBITED WITH THIADIAZOLE INHIBITOR PNU-142372

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
AIN9300

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
AHOH307
AHOH316

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 261
ChainResidue
AASP107
AASP182
AGLU184
AHOH321
AHOH331

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN A 262
ChainResidue
AHIS96
AHIS96
AHIS96
AHOH263
AHOH263
AHOH263

site_idAC7
Number of Residues13
DetailsBINDING SITE FOR RESIDUE IN9 A 300
ChainResidue
ATYR155
AHIS166
AALA167
ATYR168
AALA169
ATHR190
ATHR191
AGLU202
AHIS205
AHIS211
AZN257
AHOH320
AHOH380

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 Residues8
DetailsSITE INH IS THE BINDING SITE FOR THE UREA-THIADIAZOLE INHIBITOR PNU-142372; IN9 300.
ChainResidue
APHE86
ATYR155
AHIS166
AALA167
ATYR168
AALA169
AHIS205
APHE210

site_idZN1
Number of Residues4
DetailsZN1 ARE THE LIGANDS OF THE CATALYTIC (ZN 257) ZINC ION.
ChainResidue
AHIS205
AHIS211
AIN9300
AHIS201

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

219140

PDB entries from 2024-05-01

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