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1D5J

CRYSTAL STRUCTURE OF MMP3 COMPLEXED WITH A THIAZEPINE 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 Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 301
ChainResidue
AHIS201
AHIS205
AHIS211
AMM3401

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
AGLY159
AGLY161
AVAL163
AASP181
AGLU184
AASP158

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA A 304
ChainResidue
AASP107
AASP182
AGLU184
AHOH449

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA A 305
ChainResidue
AALA140
AASP141
AGLY173
AASN175
AASP177
AHOH408
AHOH412

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 801
ChainResidue
BHIS701
BHIS705
BHIS711
BMM3901

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 802
ChainResidue
BHIS651
BASP653
BHIS666
BHIS679

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 803
ChainResidue
BASP658
BGLY659
BGLY661
BVAL663
BASP681
BGLU684

site_idAC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA B 804
ChainResidue
BHOH14
BHOH21
BASP607
BASP682
BGLU684

site_idBC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA B 805
ChainResidue
BHOH16
BASP641
BGLY673
BASN675
BASP677

site_idBC2
Number of Residues14
DetailsBINDING SITE FOR RESIDUE MM3 A 401
ChainResidue
AASN162
AVAL163
ALEU164
AALA165
ALEU197
AVAL198
AHIS201
AGLU202
AHIS205
AHIS211
APRO221
ALEU222
ATYR223
AZN301

site_idBC3
Number of Residues11
DetailsBINDING SITE FOR RESIDUE MM3 B 901
ChainResidue
BARG593
BVAL663
BLEU664
BALA665
BVAL698
BHIS701
BGLU702
BHIS705
BHIS711
BTYR723
BZN801

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
BGLU702

site_idSWS_FT_FI2
Number of Residues32
DetailsBINDING:
ChainResidueDetails
AASP107
AGLY173
AASN175
AASP177
AHIS179
AASP181
AASP182
AGLU184
BASP607
BASP641
BHIS651
AASP141
BASP653
BASP658
BGLY659
BGLY661
BVAL663
BHIS666
BGLY673
BASN675
BASP677
BHIS679
AHIS151
BASP681
BASP682
BGLU684
AASP153
AASP158
AGLY159
AGLY161
AVAL163
AHIS166

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:8740360
ChainResidueDetails
AHIS201
AHIS205
AHIS211
BHIS701
BHIS705
BHIS711

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
BGLU702
BMET719

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
BGLU702

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
BHIS701metal ligand
BGLU702proton acceptor, proton donor
BHIS705metal ligand
BHIS711metal ligand

221716

PDB entries from 2024-06-26

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