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2OW9

Crystal structure analysis of the MMP13 catalytic domain in complex with specific 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 601
ChainResidue
AHIS201
AHIS205
AHIS211
AHAE502
AHOH836

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 602
ChainResidue
AHIS151
AASP153
AHIS166
AHIS179

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 603
ChainResidue
AASP158
AGLY159
ASER161
ALEU163
AASP181
AGLU184

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 604
ChainResidue
AASP141
AASN173
AGLY175
AASP177
AHOH702
AHOH726

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CA A 605
ChainResidue
AASP107
AASP182
AGLU184

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 606
ChainResidue
BHIS201
BHIS205
BHIS211
BHAE502

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 607
ChainResidue
BHIS151
BASP153
BHIS166
BHIS179

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 608
ChainResidue
BASP158
BGLY159
BSER161
BLEU163
BASP181
BGLU184

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 609
ChainResidue
BASP141
BASN173
BGLY175
BASP177
BHOH621
BHOH630

site_idBC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA B 610
ChainResidue
BASP107
BASP182
BGLU184
BHOH629
BHOH653

site_idBC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA B 611
ChainResidue
BHIS110
BGLU114
BHIS230
BHOH789
BHOH790

site_idBC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 701
ChainResidue
ALYS118
AARG134
AHOH713
AHOH722
AHOH802
AHOH808
AHOH893

site_idBC4
Number of Residues16
DetailsBINDING SITE FOR RESIDUE SP6 A 501
ChainResidue
ALEU197
AHIS201
AALA217
ALEU218
APHE220
AILE222
ATYR223
ATHR224
ATYR225
ATHR226
ALYS228
ASER229
AHIS230
APHE231
AMET232
AHOH712

site_idBC5
Number of Residues17
DetailsBINDING SITE FOR RESIDUE SP6 B 501
ChainResidue
BLEU197
BHIS201
BALA217
BLEU218
BPHE220
BILE222
BTYR223
BTHR224
BTYR225
BTHR226
BLYS228
BSER229
BHIS230
BPHE231
BMET232
BHAE502
BHOH635

site_idBC6
Number of Residues8
DetailsBINDING SITE FOR RESIDUE HAE A 502
ChainResidue
AZN601
AHOH708
AHOH836
AALA165
AHIS201
AGLU202
AHIS205
AHIS211

site_idBC7
Number of Residues8
DetailsBINDING SITE FOR RESIDUE HAE B 502
ChainResidue
BALA165
BHIS201
BGLU202
BHIS211
BPRO221
BSP6501
BZN606
BHOH663

Functional Information from PROSITE/UniProt
site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. VAAHEFGHSL
ChainResidueDetails
AVAL198-LEU207

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000305|PubMed:23913860
ChainResidueDetails
AGLU202
BGLU202

site_idSWS_FT_FI2
Number of Residues24
DetailsBINDING: BINDING => ECO:0000269|PubMed:10926524, ECO:0000269|PubMed:10986126, ECO:0000269|PubMed:15734645, ECO:0000269|PubMed:15780611, ECO:0000269|PubMed:17196980, ECO:0000269|PubMed:17623656, ECO:0000269|PubMed:19422229, ECO:0000269|PubMed:20005097, ECO:0000269|PubMed:20726512, ECO:0000269|PubMed:22689580, ECO:0000269|PubMed:23810497, ECO:0000269|PubMed:23913860, ECO:0000269|PubMed:8969305
ChainResidueDetails
AASP107
ASER161
ALEU163
AASN173
AGLY175
AASP177
AASP181
AASP182
AGLU184
BASP107
BASP141
BASP158
BGLY159
BSER161
BLEU163
BASN173
BGLY175
BASP177
BASP181
BASP182
BGLU184
AASP141
AASP158
AGLY159

site_idSWS_FT_FI3
Number of Residues16
DetailsBINDING: BINDING => ECO:0000269|PubMed:10926524, ECO:0000269|PubMed:10986126, ECO:0000269|PubMed:15734645, ECO:0000269|PubMed:15780611, ECO:0000269|PubMed:17196980, ECO:0000269|PubMed:17623656, ECO:0000269|PubMed:19422229, ECO:0000269|PubMed:20005097, ECO:0000269|PubMed:20726512, ECO:0000269|PubMed:22689580, ECO:0000269|PubMed:23810497, ECO:0000269|PubMed:23913860
ChainResidueDetails
AHIS211
AMET219
BHIS151
BASP153
BHIS166
BHIS179
BHIS201
BHIS205
BHIS211
BMET219
AHIS151
AASP153
AHIS166
AHIS179
AHIS201
AHIS205

site_idSWS_FT_FI4
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:8576151
ChainResidueDetails
AASN96
BASN96

site_idSWS_FT_FI5
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN131
BASN131

218500

건을2024-04-17부터공개중

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