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6GJK

A degradation product of PD 404182 (P2742) bound to Histone Deacetylase-like Amidohydrolase

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 401
ChainResidue
AASP180
AHIS182
AASP268
AACT409

site_idAC2
Number of Residues5
Detailsbinding site for residue K A 402
ChainResidue
AASP178
AASP180
AHIS182
ASER201
ALEU202

site_idAC3
Number of Residues7
Detailsbinding site for residue K A 403
ChainResidue
ATRP191
AASP194
AVAL197
ATHR199
ATYR226
AHOH607
AHOH617

site_idAC4
Number of Residues5
Detailsbinding site for residue 1PE A 404
ChainResidue
AARG173
APRO195
ATYR226
AHOH835
AHOH849

site_idAC5
Number of Residues3
Detailsbinding site for residue PEG A 405
ChainResidue
AARG355
AHOH852
BTHR349

site_idAC6
Number of Residues5
Detailsbinding site for residue PEG A 406
ChainResidue
AASN185
AGLN188
AASP189
ATRP192
AHOH553

site_idAC7
Number of Residues7
Detailsbinding site for residue F0Z A 407
ChainResidue
ACYS51
AILE56
AGLU57
AMLT410
AHOH752
BTHR9
BPEG406

site_idAC8
Number of Residues4
Detailsbinding site for residue F0Z A 408
ChainResidue
AARG254
ACYS295
AASP298
AILE299

site_idAC9
Number of Residues9
Detailsbinding site for residue ACT A 409
ChainResidue
AHIS142
AHIS143
AGLY151
AASP180
AHIS182
AASP268
AGLY310
ATYR312
AZN401

site_idAD1
Number of Residues8
Detailsbinding site for residue MLT A 410
ChainResidue
AHIS47
AF0Z407
AHOH522
AHOH548
AHOH667
AHOH713
BHIS47
BF0Z409

site_idAD2
Number of Residues4
Detailsbinding site for residue ZN B 401
ChainResidue
BASP180
BHIS182
BASP268
BACT411

site_idAD3
Number of Residues5
Detailsbinding site for residue K B 402
ChainResidue
BASP178
BASP180
BHIS182
BSER201
BLEU202

site_idAD4
Number of Residues7
Detailsbinding site for residue K B 403
ChainResidue
BTRP191
BASP194
BVAL197
BTHR199
BTYR226
BHOH626
BHOH646

site_idAD5
Number of Residues8
Detailsbinding site for residue 1PE B 404
ChainResidue
BGLU172
BARG173
BPRO195
BASN222
BHOH505
BHOH667
BHOH739
BHOH796

site_idAD6
Number of Residues3
Detailsbinding site for residue PEG B 405
ChainResidue
BARG355
BHOH673
BHOH680

site_idAD7
Number of Residues5
Detailsbinding site for residue PEG B 406
ChainResidue
AF0Z407
AHOH667
BTRP7
BPRO61
BILE62

site_idAD8
Number of Residues3
Detailsbinding site for residue PEG B 407
ChainResidue
BGLN188
BTRP192
BASP211

site_idAD9
Number of Residues5
Detailsbinding site for residue PEG B 408
ChainResidue
BARG74
BHIS146
BASP189
BILE190
BHOH536

site_idAE1
Number of Residues9
Detailsbinding site for residue ACT B 411
ChainResidue
BGLY151
BASP180
BHIS182
BASP268
BGLY310
BTYR312
BZN401
BHIS142
BHIS143

site_idAE2
Number of Residues14
Detailsbinding site for Di-peptide F0Z B 409 and CYS B 51
ChainResidue
ATRP7
ATHR9
AMLT410
BHIS47
BGLU48
BLEU49
BVAL50
BALA52
BSER53
BGLY54
BILE56
BGLU57
BHOH577
BHOH734

site_idAE3
Number of Residues12
Detailsbinding site for Di-peptide F0Z B 410 and CYS B 295
ChainResidue
BLEU250
BARG254
BARG291
BTHR292
BILE293
BASP294
BALA296
BALA297
BASP298
BILE299
BHOH530
BHOH595

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 2024-07-10

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