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4L19

Matrix metalloproteinase-13 complexed with selective inhibitor compound Q1

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
AHIS172
AASP174
AHIS187
AHIS200

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 302
ChainResidue
AHIS222
AHIS226
AHIS232
AFMT306

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 303
ChainResidue
ASER250
AHIS251
AGOL309
AHIS131

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 304
ChainResidue
AASP179
AGLY180
ASER182
ALEU184
AASP202
AGLU205

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 305
ChainResidue
AASP162
AASN194
AGLY196
AASP198
AHOH407
AHOH458

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FMT A 306
ChainResidue
AHIS222
AGLU223
AHIS226
AHIS232
AZN302
A1UA308

site_idAC7
Number of Residues8
DetailsBINDING SITE FOR RESIDUE 1UA A 307
ChainResidue
ALEU218
AHIS222
ALEU239
APHE241
AILE243
ATHR245
ATHR247
APHE252

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE 1UA A 308
ChainResidue
ATYR176
AALA188
APHE189
AHIS226
AFMT306
AHOH494

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 309
ChainResidue
AHIS131
AGLU135
AARG155
ASER250
AZN303
BPRO127

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 301
ChainResidue
BHIS172
BASP174
BHIS187
BHIS200

site_idBC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 302
ChainResidue
BHIS222
BHIS226
BHIS232
BFMT305

site_idBC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 303
ChainResidue
BASP162
BASN194
BGLY196
BASP198
BHOH489
BHOH505

site_idBC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 304
ChainResidue
BASP179
BGLY180
BSER182
BLEU184
BASP202
BGLU205

site_idBC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FMT B 305
ChainResidue
BHIS222
BGLU223
BHIS226
BHIS232
BZN302
BHOH458

site_idBC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FMT B 306
ChainResidue
ATHR130
AHIS131
BTHR130
BHIS131
BHOH408

site_idBC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE FMT B 307
ChainResidue
BLYS234
BGLN263
BHOH442
BHOH464

site_idBC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE FMT B 308
ChainResidue
BLYS115
BMET116
BASN117
BHOH460

site_idBC9
Number of Residues8
DetailsBINDING SITE FOR RESIDUE 1UA B 309
ChainResidue
BHIS222
BGLY237
BLEU239
BPHE241
BILE243
BTYR244
BTHR245
BPHE252

site_idCC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL B 310
ChainResidue
BHOH493
BHOH555
BTYR176
BALA188

site_idCC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL B 311
ChainResidue
BARG155
BLEU156
BHIS157
BASP158
BHOH413
BHOH498

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

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

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

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PDB entries from 2024-05-01

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