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4H2E

Crystal structure of an MMP twin inhibitor complexing two MMP-9 catalytic domains

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
B0Y3306

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

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA A 303
ChainResidue
AGLY197
AGLN199
AASP201
AASP165

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 304
ChainResidue
AASP182
AGLY183
AASP185
ALEU187
AASP205
AGLU208

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE PEG A 305
ChainResidue
ALYS258
BALA146

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PEG A 306
ChainResidue
AGLU241
AHOH425
BPEG308
BHOH460

site_idAC7
Number of Residues1
DetailsBINDING SITE FOR RESIDUE PEG A 307
ChainResidue
APEG308

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PEG A 308
ChainResidue
ATYR179
APEG307
AHOH420

site_idAC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PEG A 309
ChainResidue
AALA173
AGLU174
APHE181
AACT312
ABCN314

site_idBC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE PEG A 310
ChainResidue
AASN127
AVAL172

site_idBC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE ACT A 311
ChainResidue
AHOH440

site_idBC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE ACT A 312
ChainResidue
APEG309

site_idBC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE ACT A 313
ChainResidue
AHOH463

site_idBC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE BCN A 314
ChainResidue
AASP182
APEG309
BARG249
BGLU252

site_idBC6
Number of Residues1
DetailsBINDING SITE FOR RESIDUE BCN A 315
ChainResidue
AHOH473

site_idBC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 301
ChainResidue
BHIS226
BHIS230
BHIS236
B0Y3306

site_idBC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 302
ChainResidue
BHIS175
BASP177
BHIS190
BHIS203

site_idBC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA B 303
ChainResidue
BALA164
BASP165
BGLY197
BGLN199
BASP201

site_idCC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 304
ChainResidue
BASP182
BGLY183
BASP185
BLEU187
BASP205
BGLU208

site_idCC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA B 305
ChainResidue
BSER129
BASP131
BASP206
BGLU208
BTRP210

site_idCC3
Number of Residues33
DetailsBINDING SITE FOR RESIDUE 0Y3 B 306
ChainResidue
BHOH459
ALEU187
ALEU188
AALA189
ALEU222
AHIS226
AGLU227
AHIS230
AASP235
AHIS236
ALEU243
ATYR245
APRO246
ATYR248
AZN301
BGLY106
BPHE107
BLEU188
BALA189
BLEU222
BVAL223
BHIS226
BGLU227
BHIS230
BASP235
BHIS236
BLEU243
BTYR245
BPRO246
BMET247
BTYR248
BZN301
BHOH437

site_idCC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE PEG B 307
ChainResidue
BPEG308

site_idCC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PEG B 308
ChainResidue
APEG306
BPRO180
BPEG307
BPEG309

site_idCC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PEG B 309
ChainResidue
BGLY178
BTYR179
BPEG308

site_idCC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ACT B 310
ChainResidue
BPHE250
BTHR251
BGLU252
BHOH458

site_idCC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE BCN B 311
ChainResidue
BALA173
BGLU174
BPRO180
BPHE181
BHOH449
BHOH457

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

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PDB entries from 2024-07-10

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