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2OW1

MMP-9 active site mutant with trifluoromethyl hydroxamate 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 444
ChainResidue
AHIS401
AHIS405
AHIS411
A7MR501

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 445
ChainResidue
AHIS175
AASP177
AHIS190
AHIS203

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 444
ChainResidue
BHIS405
BHIS411
B7MR502
BHIS401

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 445
ChainResidue
BHIS175
BASP177
BHIS190
BHIS203

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 446
ChainResidue
AASP182
AGLY183
AASP185
ALEU187
AASP205
AGLU208

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 447
ChainResidue
AASP165
AGLY197
AGLN199
AASP201
AHOH505
AHOH594

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA A 448
ChainResidue
ASER129
AASP131
AASP206
AGLU208

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA A 449
ChainResidue
ASER149
ATHR152
AHOH532
AHOH576

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 446
ChainResidue
BASP182
BGLY183
BASP185
BLEU187
BASP205
BGLU208

site_idBC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA B 447
ChainResidue
BASP165
BGLY197
BGLN199
BASP201
BHOH508

site_idBC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA B 448
ChainResidue
BASP131
BASP206
BGLU208
BHOH568

site_idBC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA B 449
ChainResidue
BSER149
BTHR152
BHOH543
BHOH583

site_idBC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 450
ChainResidue
AASN127
ATYR128
BTYR128

site_idBC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 451
ChainResidue
AASN127
AGLN169
APHE170
AHOH543

site_idBC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 452
ChainResidue
AGLY213
ASER394
BHOH509

site_idBC7
Number of Residues15
DetailsBINDING SITE FOR RESIDUE 7MR A 501
ChainResidue
AGLY186
ALEU188
AALA189
AHIS401
AGLN402
AHIS405
AHIS411
ALEU418
ATYR420
APRO421
AMET422
ATYR423
AARG424
AZN444
AHOH551

site_idBC8
Number of Residues15
DetailsBINDING SITE FOR RESIDUE 7MR B 502
ChainResidue
BLEU187
BLEU188
BALA189
BHIS401
BGLN402
BHIS405
BHIS411
BLEU418
BTYR420
BPRO421
BMET422
BTYR423
BARG424
BZN444
BHOH532

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000269|PubMed:12051944
ChainResidueDetails
AGLN402
BGLN402

site_idSWS_FT_FI2
Number of Residues24
DetailsBINDING: BINDING => ECO:0000269|PubMed:12051944
ChainResidueDetails
AASP131
AASP205
AASP206
AGLU208
BASP131
BASP165
BASP182
BGLY183
BASP185
BLEU187
BGLY197
AASP165
BGLN199
BASP201
BASP205
BASP206
BGLU208
AASP182
AGLY183
AASP185
ALEU187
AGLY197
AGLN199
AASP201

site_idSWS_FT_FI3
Number of Residues14
DetailsBINDING: BINDING => ECO:0000269|PubMed:12051944, ECO:0000269|PubMed:12077439
ChainResidueDetails
AHIS175
BHIS190
BHIS203
BHIS401
BHIS405
BHIS411
AASP177
AHIS190
AHIS203
AHIS401
AHIS405
AHIS411
BHIS175
BASP177

site_idSWS_FT_FI4
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN120
AASN127
BASN120
BASN127

220113

PDB entries from 2024-05-22

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