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2HU2

CTBP/BARS in ternary complex with NAD(H) and RRTGAPPAL peptide

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003714molecular_functiontranscription corepressor activity
A0005634cellular_componentnucleus
A0016491molecular_functionoxidoreductase activity
A0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A0045892biological_processnegative regulation of DNA-templated transcription
A0051287molecular_functionNAD binding
Functional Information from PDB Data
site_idAC1
Number of Residues26
DetailsBINDING SITE FOR RESIDUE NAD A 600
ChainResidue
ASER89
AASP193
APRO194
ATYR195
AHIS225
ACYS226
AGLY227
AASN229
AASN232
ATHR253
AALA254
AGLY90
AARG255
AASP279
AHIS304
AALA306
ATRP307
AHOH506
AHOH517
ATHR117
AILE169
AGLY170
AGLY172
AARG173
AVAL174
ATYR192

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FMT A 801
ChainResidue
ATYR65
AHIS66
AARG86
AILE87
ATRP307

Functional Information from PROSITE/UniProt
site_idPS00065
Number of Residues28
DetailsD_2_HYDROXYACID_DH_1 D-isomer specific 2-hydroxyacid dehydrogenases NAD-binding signature. LGIIGlGRVGqavalrakafgfn.VLfYD
ChainResidueDetails
ALEU166-ASP193

site_idPS00671
Number of Residues17
DetailsD_2_HYDROXYACID_DH_3 D-isomer specific 2-hydroxyacid dehydrogenases signature 3. MRqGaFLVNtARGgLVD
ChainResidueDetails
AMET244-ASP260

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000250
ChainResidueDetails
AARG255
AGLU284

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000250
ChainResidueDetails
AHIS304

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:12805226, ECO:0000269|PubMed:16940172
ChainResidueDetails
ASER89
AILE169
AASP193
ACYS226
ATHR253
AASP279

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q13363
ChainResidueDetails
ASER289

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1psd
ChainResidueDetails
AHIS304
AGLU284

224004

PDB entries from 2024-08-21

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