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5CUH

Crystal structure MMP-9 complexes with a constrained hydroxamate based inhibitor LT4

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
ALTQ306

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
AHOH439
AHOH441
AASP165

site_idAC4
Number of Residues6
Detailsbinding site for residue CA A 304
ChainResidue
AASP131
AASP206
AGLU208
AHOH482
AHOH512
AHOH533

site_idAC5
Number of Residues6
Detailsbinding site for residue CA A 305
ChainResidue
AASP182
AGLY183
AASP185
ALEU187
AASP205
AGLU208

site_idAC6
Number of Residues17
Detailsbinding site for residue LTQ A 306
ChainResidue
ALEU187
ALEU188
AALA189
ALEU222
AHIS226
AGLU227
AHIS230
AHIS236
ALEU243
ATYR245
AMET247
ATYR248
AZN301
AHOH419
BTYR245
BPRO246
BMET247

site_idAC7
Number of Residues3
Detailsbinding site for residue EDO A 307
ChainResidue
AASP177
AGLY178
ATYR179

site_idAC8
Number of Residues3
Detailsbinding site for residue EDO A 308
ChainResidue
AGLY183
ALYS184
AASP207

site_idAC9
Number of Residues4
Detailsbinding site for residue PGO A 309
ChainResidue
AHIS190
AALA191
APHE192
AHOH442

site_idAD1
Number of Residues4
Detailsbinding site for residue ZN B 301
ChainResidue
BHIS226
BHIS230
BHIS236
BLTQ306

site_idAD2
Number of Residues4
Detailsbinding site for residue ZN B 302
ChainResidue
BHIS175
BASP177
BHIS190
BHIS203

site_idAD3
Number of Residues6
Detailsbinding site for residue CA B 303
ChainResidue
BASP165
BGLY197
BGLN199
BASP201
BHOH429
BHOH436

site_idAD4
Number of Residues5
Detailsbinding site for residue CA B 304
ChainResidue
BASP131
BASP206
BGLU208
BHOH528
BHOH553

site_idAD5
Number of Residues6
Detailsbinding site for residue CA B 305
ChainResidue
BASP182
BGLY183
BASP185
BLEU187
BASP205
BGLU208

site_idAD6
Number of Residues18
Detailsbinding site for residue LTQ B 306
ChainResidue
ATYR245
APRO246
BGLY186
BLEU187
BLEU188
BALA189
BLEU222
BHIS226
BGLU227
BHIS230
BHIS236
BLEU243
BTYR245
BMET247
BTYR248
BARG249
BZN301
BHOH462

site_idAD7
Number of Residues3
Detailsbinding site for residue EDO B 307
ChainResidue
BASP177
BGLY178
BTYR179

site_idAD8
Number of Residues4
Detailsbinding site for residue EDO B 308
ChainResidue
AARG162
BGLY183
BASP207
BHOH526

site_idAD9
Number of Residues4
Detailsbinding site for residue DMS B 309
ChainResidue
AHOH428
BHIS190
BALA191
BPHE192

site_idAE1
Number of Residues2
Detailsbinding site for residue PGO B 310
ChainResidue
BALA135
BASP139

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
AGLU227
BGLU227

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
BHIS226
BHIS230
BHIS236
AASP177
AHIS190
AHIS203
AHIS226
AHIS230
AHIS236
BHIS175
BASP177

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

223790

PDB entries from 2024-08-14

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