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4H3X

Crystal structure of an MMP broad spectrum hydroxamate based inhibitor CC27 in complex with the MMP-9 catalytic domain

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
A10B306

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
AGLY183
AASP185
ALEU187
AASP205
AGLU208
AASP182

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 304
ChainResidue
AASP131
AASP206
AGLU208
AHOH452
AHOH453

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 305
ChainResidue
AASP165
AGLY197
AGLN199
AASP201
AHOH406
AHOH411

site_idAC6
Number of Residues17
DetailsBINDING SITE FOR RESIDUE 10B A 306
ChainResidue
AGLY186
ALEU187
ALEU188
AALA189
ALEU222
AHIS226
AGLU227
AHIS230
AHIS236
ALEU243
ATYR245
AMET247
AZN301
AHOH415
AHOH492
BTYR245
BPRO246

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 307
ChainResidue
APRO254
AHOH421
BPRO254
BPRO255
BHOH448
BHOH451

site_idAC8
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 308
ChainResidue
AASP177
AGLY178
AGOL311
AHOH476
AHOH515
AHOH553
AHOH559
AHOH560
AHOH590

site_idAC9
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 309
ChainResidue
ATYR179
ALEU187
AHIS190
AHOH594
AHOH595
BPRO240
BTYR245

site_idBC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE PGO A 310
ChainResidue
AALA173
AGLU174

site_idBC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 311
ChainResidue
AGOL308
AHOH480
AHOH515
AHOH529
AHOH553

site_idBC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 312
ChainResidue
AASN120
ATHR122
ATHR157
AHOH536

site_idBC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE GOL A 313
ChainResidue
AHOH434
AHOH483

site_idBC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 301
ChainResidue
BHIS226
BHIS230
BHIS236
B10B306

site_idBC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 302
ChainResidue
BHIS175
BASP177
BHIS190
BHIS203

site_idBC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 303
ChainResidue
BASP182
BGLY183
BASP185
BLEU187
BASP205
BGLU208

site_idBC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA B 304
ChainResidue
BASP131
BASP206
BGLU208
BHOH468
BHOH529

site_idBC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 305
ChainResidue
BASP201
BHOH401
BHOH405
BASP165
BGLY197
BGLN199

site_idCC1
Number of Residues18
DetailsBINDING SITE FOR RESIDUE 10B B 306
ChainResidue
ATYR245
APRO246
AMET247
BGLY186
BLEU187
BLEU188
BALA189
BLEU222
BHIS226
BGLU227
BHIS230
BHIS236
BLEU243
BTYR245
BMET247
BTYR248
BZN301
BHOH444

site_idCC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL B 307
ChainResidue
BPHE250
BTHR251
BHOH423
BHOH515
BHOH546

site_idCC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PEG B 308
ChainResidue
BPEG309
BHOH442
BHOH443
BHOH480

site_idCC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PEG B 309
ChainResidue
BTYR179
BPEG308
BHOH442

Functional Information from PROSITE/UniProt
site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. VAAHEFGHAL
ChainResidueDetails
AVAL223-LEU232

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000269|PubMed:12051944
ChainResidueDetails
BGLU227
AGLU227

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

site_idSWS_FT_FI3
Number of Residues14
DetailsBINDING: BINDING => ECO:0000269|PubMed:12051944, ECO:0000269|PubMed:12077439
ChainResidueDetails
AHIS236
BHIS175
BASP177
BHIS190
BHIS203
BHIS226
BHIS230
BHIS236
AHIS175
AASP177
AHIS190
AHIS203
AHIS226
AHIS230

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

221051

PDB entries from 2024-06-12

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