Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

1BM6

SOLUTION STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN STROMELYSIN-1 COMPLEXED TO A POTENT NON-PEPTIDIC INHIBITOR, NMR, 20 STRUCTURES

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 Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 256
ChainResidue
AHAV1
AHIS201
AHIS205
AHIS211
AMET219

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 257
ChainResidue
AHIS151
APHE157
AHIS166
AHIS179

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 258
ChainResidue
AASP158
AGLY159
AGLY161
AVAL163
AASP181
AGLU184

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 259
ChainResidue
AASP141
AGLY173
AILE174
AASN175
AGLY176
AASP177

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE HAV A 1
ChainResidue
A3MP2
AMSB3
AVAL163
AALA165
AHIS201
AHIS205
AZN256

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE 3MP A 2
ChainResidue
AHAV1
AMSB3
AASN162

site_idAC7
Number of Residues14
DetailsBINDING SITE FOR RESIDUE MSB A 3
ChainResidue
AHAV1
A3MP2
AASN162
AVAL163
ALEU164
AALA165
ALEU197
AVAL198
AHIS201
ALEU218
AMET219
ATYR220
APRO221
ALEU222

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

226707

PDB entries from 2024-10-30

PDB statisticsPDBj update infoContact PDBjnumon