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

3WV2

Crystal structure of the catalytic domain of MMP-13 complexed with N-(3-methoxybenzyl)-4-oxo-3,4-dihydroquinazoline-2-carboxamide

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
AHIS222
AHIS226
AHIS232
AHOH602

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 302
ChainResidue
AHIS172
AASP174
AHIS187
AHIS200

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 303
ChainResidue
AGLY180
ASER182
ALEU184
AASP202
AGLU205
AASP179

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 304
ChainResidue
AASP162
AASN194
AGLY196
AASP198
AHOH693
AHOH695

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE NA A 305
ChainResidue
AASP128
AASP203
AGLU205

site_idAC6
Number of Residues17
DetailsBINDING SITE FOR RESIDUE WGG A 306
ChainResidue
ALEU218
AVAL219
AHIS222
AGLU223
AALA238
ALEU239
APHE241
APRO242
AILE243
ATYR244
ATHR245
ATYR246
ATHR247
APHE252
AMET253
APRO255
AHOH615

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 301
ChainResidue
BHIS222
BHIS226
BHIS232
BHOH473

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 302
ChainResidue
BHIS172
BASP174
BHIS187
BHIS200

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 303
ChainResidue
BASP179
BGLY180
BSER182
BLEU184
BASP202
BGLU205

site_idBC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 304
ChainResidue
BASP162
BASN194
BGLY196
BASP198
BHOH470
BHOH489

site_idBC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA B 305
ChainResidue
BASP128
BASP203
BGLU205
BHOH476
BHOH486

site_idBC3
Number of Residues13
DetailsBINDING SITE FOR RESIDUE WGG B 306
ChainResidue
BLEU218
BHIS222
BGLU223
BALA238
BLEU239
BPHE241
BILE243
BTYR244
BTHR245
BTHR247
BPHE252
BMET253
BHOH411

Functional Information from PROSITE/UniProt
site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. VAAHEFGHSL
ChainResidueDetails
AVAL219-LEU228

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000305|PubMed:23913860
ChainResidueDetails
AGLU223
BGLU223

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
ASER182
ALEU184
AASN194
AGLY196
AASP198
AASP202
AASP203
AGLU205
BASP128
BASP162
BASP179
BGLY180
BSER182
BLEU184
BASN194
BGLY196
BASP198
BASP202
BASP203
BGLU205
AASP128
AASP162
AASP179
AGLY180

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
AHIS232
AMET240
BHIS172
BASP174
BHIS187
BHIS200
BHIS222
BHIS226
BHIS232
BMET240
AHIS187
AHIS200
AHIS172
AASP174
AHIS222
AHIS226

site_idSWS_FT_FI4
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:8576151
ChainResidueDetails
AASN117
BASN117

site_idSWS_FT_FI5
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN152
BASN152

221051

PDB entries from 2024-06-12

PDB statisticsPDBj update infoContact PDBjnumon