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1MX3

Crystal structure of CtBP dehydrogenase core holo form

Functional Information from GO Data
ChainGOidnamespacecontents
A0003714molecular_functiontranscription corepressor activity
A0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A0051287molecular_functionNAD binding
Functional Information from PDB Data
site_idAC1
Number of Residues37
DetailsBINDING SITE FOR RESIDUE NAD A 1000
ChainResidue
ASER100
AASP204
APRO205
ATYR206
AHIS236
ACYS237
AGLY238
AASN240
AASN243
ATHR264
AALA265
AGLY101
AARG266
AASP290
AVAL291
AHIS315
AALA317
ATRP318
AHOH2008
AHOH2011
AHOH2012
AHOH2014
ATHR128
AHOH2059
AHOH2086
AHOH2192
AHOH2264
AHOH2347
AHOH2349
AHOH2360
AACY4000
AILE180
AGLY181
AGLY183
AARG184
AVAL185
ATYR203

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE ACY A 4000
ChainResidue
AARG97
ASER100
AGLY101
AARG266
AHIS315
ANAD1000
AHOH2349
AHOH2354

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
ALEU177-ASP204

site_idPS00671
Number of Residues17
DetailsD_2_HYDROXYACID_DH_3 D-isomer specific 2-hydroxyacid dehydrogenases signature 3. MRqGaFLVNtARGgLVD
ChainResidueDetails
AMET255-ASP271

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000250
ChainResidueDetails
AARG266
AGLU295

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000250
ChainResidueDetails
AHIS315

site_idSWS_FT_FI3
Number of Residues7
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
ASER100
AILE180
AASP204
ACYS237
ATHR264
AASP290
AHIS315

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:17525332, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER300

220113

PDB entries from 2024-05-22

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