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4H1Q

Crystal structure of mutant MMP-9 catalytic domain in complex with a twin 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
AHIS226
AHIS230
AHIS236
A0XX307

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 302
ChainResidue
AHIS175
AASP177
AHIS190
AHIS203

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 303
ChainResidue
AGLY197
AGLN199
AASP201
AHOH477
AHOH481
AASP165

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA A 304
ChainResidue
AASP131
AASP206
AGLU208
AHOH421

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 305
ChainResidue
AASP182
AGLY183
AASP185
ALEU187
AASP205
AGLU208

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA A 306
ChainResidue
ASER149
ATHR152
ALEU154
AHOH496

site_idAC7
Number of Residues29
DetailsBINDING SITE FOR RESIDUE 0XX A 307
ChainResidue
ATYR179
APRO180
APHE181
AASP182
ALEU187
ALEU188
AALA189
AHIS190
AALA191
APHE192
APRO193
ALEU222
AHIS226
AGLN227
AHIS230
AHIS236
ALEU243
ATYR245
APRO246
AMET247
ATYR248
AZN301
AHOH449
AHOH526
BPRO240
BGLU241
BTYR245
BPRO246
BARG249

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 301
ChainResidue
BHIS226
BHIS230
BHIS236
B0XX306

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 302
ChainResidue
BHIS175
BASP177
BHIS190
BHIS203

site_idBC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 303
ChainResidue
BASP165
BGLY197
BGLN199
BASP201
BHOH487
BHOH489

site_idBC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA B 304
ChainResidue
BASP131
BASP206
BGLU208
BHOH517
BHOH518

site_idBC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 305
ChainResidue
BASP182
BGLY183
BASP185
BLEU187
BASP205
BGLU208

site_idBC4
Number of Residues30
DetailsBINDING SITE FOR RESIDUE 0XX B 306
ChainResidue
BHIS236
BLEU243
BTYR245
BPRO246
BMET247
BTYR248
BHIS266
BZN301
BHOH432
BHOH433
BHOH446
BHOH483
BHOH526
ATYR245
APRO246
AHOH523
BGLY112
BLEU187
BLEU188
BALA189
BHIS190
BALA191
BPRO193
BLEU222
BHIS226
BGLN227
BHIS230
BGLY233
BLEU234
BASP235

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"evidences":[{"source":"PubMed","id":"12051944","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues24
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"12051944","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues14
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"12051944","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12077439","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

251174

PDB entries from 2026-03-25

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