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4DPE

Structure of MMP3 complexed with a platinum-based 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 Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 301
ChainResidue
AHIS201
AHIS205
AHIS211
BTHR255
BHOH483

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 302
ChainResidue
AHIS151
AASP153
AHIS166
AHIS179

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 303
ChainResidue
AASP158
AGLY159
AGLY161
AVAL163
AASP181
AGLU184

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 304
ChainResidue
AASP141
AGLY173
AASN175
AASP177
AHOH402
AHOH411

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 305
ChainResidue
AASP107
AASP182
AGLU184
BHOH410
BHOH411

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PT A 306
ChainResidue
AGLU139
AMET143
AHOH460

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 301
ChainResidue
BHIS201
BHIS205
BHIS211
BNGH313

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 302
ChainResidue
BHIS151
BASP153
BHIS166
BHIS179

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 303
ChainResidue
BASP158
BGLY159
BGLY161
BVAL163
BASP181
BGLU184

site_idBC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 304
ChainResidue
BASP141
BGLY173
BASN175
BASP177
BHOH408
BHOH416

site_idBC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA B 305
ChainResidue
BASP107
BASP182
BGLU184
BHOH422

site_idBC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PT B 306
ChainResidue
BGLU139
BMET143
BHOH500
BHOH501

site_idBC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PT B 307
ChainResidue
BHIS224
BCL311
BCL312
BHOH491

site_idBC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE PT B 308
ChainResidue
BHOH494
BHOH495

site_idBC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PT B 309
ChainResidue
BARG231
BARG233
BHOH401
BHOH456
BHOH490

site_idBC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PT B 310
ChainResidue
BLYS94
BHOH402
BHOH403
BHOH404

site_idBC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL B 311
ChainResidue
BHIS224
BPT307
BCL312
BHOH491

site_idBC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL B 312
ChainResidue
BPT307
BCL311
BHOH491

site_idCC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE NGH B 313
ChainResidue
BVAL163
BLEU164
BALA165
BHIS201
BGLU202
BHIS205
BHIS211
BPRO221
BTYR223
BZN301
BHOH426

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
DetailsActive site: {}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues32
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"8740360","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
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

238895

PDB entries from 2025-07-16

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