Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

5G17

Bordetella Alcaligenes HDAH (T101A) bound to 9,9,9-trifluoro-8,8- dihydroxy-N-phenylnonanamide.

Functional Information from GO Data
ChainGOidnamespacecontents
A0000122biological_processnegative regulation of transcription by RNA polymerase II
A0004407molecular_functionhistone deacetylase activity
A0005737cellular_componentcytoplasm
A0006338biological_processchromatin remodeling
A0016787molecular_functionhydrolase activity
A0046872molecular_functionmetal ion binding
B0000122biological_processnegative regulation of transcription by RNA polymerase II
B0004407molecular_functionhistone deacetylase activity
B0005737cellular_componentcytoplasm
B0006338biological_processchromatin remodeling
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
A6DK373

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

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE K A 372
ChainResidue
ATRP191
AASP194
AVAL197
ATYR226
AHOH2296
AHOH2303

site_idAC4
Number of Residues16
DetailsBINDING SITE FOR RESIDUE 6DK A 373
ChainResidue
APRO140
AHIS142
AHIS143
AGLY151
APHE152
ACYS153
AASP180
AHIS182
APHE208
AASP268
AGLU309
AGLY310
ATYR312
APHE341
AZN370
AHOH2103

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 370
ChainResidue
BASP180
BHIS182
BASP268
B6DK373

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE K B 371
ChainResidue
BASP178
BASP180
BHIS182
BSER201
BLEU202

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE K B 372
ChainResidue
BTRP191
BASP194
BVAL197
BTYR226
BHOH2297
BHOH2306

site_idAC8
Number of Residues15
DetailsBINDING SITE FOR RESIDUE 6DK B 373
ChainResidue
BPRO140
BHIS142
BHIS143
BGLY151
BPHE152
BCYS153
BASP180
BHIS182
BPHE208
BASP268
BGLU309
BGLY310
BTYR312
BPHE341
BZN370

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

221371

PDB entries from 2024-06-19

PDB statisticsPDBj update infoContact PDBjnumon