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5G1C

Structure of HDAC like protein from Bordetella Alcaligenes bound the photoswitchable pyrazole Inhibitor CEW395

Functional Information from GO Data
ChainGOidnamespacecontents
A0016787molecular_functionhydrolase activity
A0046872molecular_functionmetal ion binding
B0016787molecular_functionhydrolase activity
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 370
ChainResidue
AASP180
AHIS182
AASP268
A9RB373

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE K A 371
ChainResidue
AASP178
AASP180
AHIS182
ASER201
ALEU202

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE K A 372
ChainResidue
ATRP191
AASP194
AVAL197
ATHR199
ATYR226
AHOH2300
AHOH2309

site_idAC4
Number of Residues14
DetailsBINDING SITE FOR RESIDUE 9RB A 373
ChainResidue
ALEU21
AHIS142
AHIS143
AGLY151
APHE152
AASP180
AHIS182
APHE208
AASP268
ATYR312
APHE341
AZN370
AHOH2275
AHOH2295

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE 1PE A 374
ChainResidue
AARG173
APRO195
AASN222
ATYR226
AARG369
AHOH2289
AHOH2484

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PEG A 375
ChainResidue
ATHR349
APEG376
AHOH2485
BHOH2475

site_idAC7
Number of Residues14
DetailsBINDING SITE FOR RESIDUE PEG A 376
ChainResidue
AHIS205
APRO231
ALEU232
APRO233
APRO234
AGLU360
APEG375
AHOH2320
AHOH2321
AHOH2470
AHOH2471
AHOH2486
AHOH2487
AHOH2488

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PEG A 377
ChainResidue
AARG355
AHOH2489
AHOH2490
AHOH2492

site_idAC9
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PEG A 378
ChainResidue
AASP352
AALA353
AHOH2464
AHOH2467
AHOH2495
BASP352
BALA353
BHOH2478

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 370
ChainResidue
BASP180
BHIS182
BASP268
B9RB373

site_idBC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE K B 371
ChainResidue
BASP178
BASP180
BHIS182
BSER201
BLEU202

site_idBC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE K B 372
ChainResidue
BTRP191
BASP194
BVAL197
BTHR199
BTYR226
BHOH2305
BHOH2314

site_idBC4
Number of Residues16
DetailsBINDING SITE FOR RESIDUE 9RB B 373
ChainResidue
BLEU21
BALA22
BHIS142
BHIS143
BGLY151
BPHE152
BASP180
BHIS182
BPHE208
BASP268
BTYR312
BPHE341
BZN370
BHOH2052
BHOH2278
BHOH2450

site_idBC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE 1PE B 374
ChainResidue
BGLU172
BARG173
BPRO195
BTYR226
BHOH2391
BHOH2488
BHOH2490
BHOH2491

site_idBC6
Number of Residues10
DetailsBINDING SITE FOR RESIDUE PEG B 375
ChainResidue
BLYS85
BSER88
BASN89
BGLY106
BGLU109
BHOH2190
BHOH2233
BHOH2234
BHOH2492
BHOH2493

site_idBC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PEG B 376
ChainResidue
BASP283
BHIS339
BHOH2366
BHOH2460
BHOH2494

site_idBC8
Number of Residues10
DetailsBINDING SITE FOR RESIDUE PEG B 377
ChainResidue
BASN238
BALA239
BLEU242
BASP283
BGLN287
BHOH2366
BHOH2367
BHOH2465
BHOH2466
BHOH2468

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor/acceptor => ECO:0000250|UniProtKB:Q48935
ChainResidueDetails
AHIS143
BHIS143

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:27756124, ECO:0007744|PDB:5G1C
ChainResidueDetails
AASP180
AHIS182
AASP268
BASP180
BHIS182
BASP268

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Polarizes the scissile carbonyl of the substrate => ECO:0000250|UniProtKB:Q48935
ChainResidueDetails
ATYR312
BTYR312

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PDB entries from 2024-07-24

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