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2D1O

Stromelysin-1 (MMP-3) complexed to a hydroxamic acid inhibitor

Functional Information from GO Data
ChainGOidnamespacecontents
A0004222molecular_functionmetalloendopeptidase activity
A0006508biological_processproteolysis
A0008237molecular_functionmetallopeptidase activity
A0008270molecular_functionzinc ion binding
A0031012cellular_componentextracellular matrix
B0004222molecular_functionmetalloendopeptidase activity
B0006508biological_processproteolysis
B0008237molecular_functionmetallopeptidase activity
B0008270molecular_functionzinc ion binding
B0031012cellular_componentextracellular matrix
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 257
ChainResidue
AHIS201
AHIS205
AHIS211
AFA41001

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
AGLY159
AGLY161
AVAL163
AASP181
AGLU184
AASP158

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CA A 260
ChainResidue
AASP107
AASP182
AGLU184

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 261
ChainResidue
AASP141
AGLY173
AASN175
AASP177
AHOH1022

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 262
ChainResidue
BHIS201
BHIS205
BHIS211
BFA41002

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 263
ChainResidue
BHIS151
BASP153
BHIS166
BHIS179

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 264
ChainResidue
BASP158
BGLY159
BGLY161
BVAL163
BASP181
BGLU184

site_idAC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CA B 265
ChainResidue
BASP107
BASP182
BGLU184

site_idBC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 266
ChainResidue
BASP141
BGLY173
BASN175
BASP177
BHOH1005
BHOH1010

site_idBC2
Number of Residues18
DetailsBINDING SITE FOR RESIDUE FA4 A 1001
ChainResidue
AASN162
AVAL163
ALEU164
AALA165
AHIS201
AGLU202
AHIS205
AHIS211
ATHR215
AALA217
ALEU218
ATYR220
ALEU222
ATYR223
AZN257
AHOH1005
AHOH1034
BHIS224

site_idBC3
Number of Residues19
DetailsBINDING SITE FOR RESIDUE FA4 B 1002
ChainResidue
AHIS224
BASN162
BVAL163
BLEU164
BALA165
BHIS201
BGLU202
BHIS205
BHIS211
BTHR215
BALA217
BLEU218
BTYR220
BLEU222
BTYR223
BZN262
BHOH1006
BHOH1030
BHOH1046

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 Residues2
DetailsACT_SITE:
ChainResidueDetails
AGLU202
BGLU202

site_idSWS_FT_FI2
Number of Residues32
DetailsBINDING:
ChainResidueDetails
AASP107
AGLY173
AASN175
AASP177
AHIS179
AASP181
AASP182
AGLU184
BASP107
BASP141
BHIS151
AASP141
BASP153
BASP158
BGLY159
BGLY161
BVAL163
BHIS166
BGLY173
BASN175
BASP177
BHIS179
AHIS151
BASP181
BASP182
BGLU184
AASP153
AASP158
AGLY159
AGLY161
AVAL163
AHIS166

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:8740360
ChainResidueDetails
AHIS201
AHIS205
AHIS211
BHIS201
BHIS205
BHIS211

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

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1hfs
ChainResidueDetails
BMET219
BGLU202

site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 1hfs
ChainResidueDetails
AGLU202

site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 1hfs
ChainResidueDetails
BGLU202

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

site_idMCSA2
Number of Residues4
DetailsM-CSA 591
ChainResidueDetails
BHIS201metal ligand
BGLU202proton acceptor, proton donor
BHIS205metal ligand
BHIS211metal ligand

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PDB entries from 2024-11-13

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