Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2OME

Crystal structure of human CTBP2 dehydrogenase complexed with NAD(H)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003714	molecular_function	transcription corepressor activity
A	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A	0051287	molecular_function	NAD binding
B	0003714	molecular_function	transcription corepressor activity
B	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
B	0051287	molecular_function	NAD binding
C	0003714	molecular_function	transcription corepressor activity
C	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
C	0051287	molecular_function	NAD binding
D	0003714	molecular_function	transcription corepressor activity
D	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
D	0051287	molecular_function	NAD binding
E	0003714	molecular_function	transcription corepressor activity
E	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
E	0051287	molecular_function	NAD binding
F	0003714	molecular_function	transcription corepressor activity
F	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
F	0051287	molecular_function	NAD binding
G	0003714	molecular_function	transcription corepressor activity
G	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
G	0051287	molecular_function	NAD binding
H	0003714	molecular_function	transcription corepressor activity
H	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
H	0051287	molecular_function	NAD binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	26
Details	BINDING SITE FOR RESIDUE NAD A 901

Chain	Residue
A	SER106
A	PRO211
A	TYR212
A	LEU213
A	HIS242
A	CYS243
A	ASN244
A	ASN246
A	ASN249
A	ALA270
A	ALA271
A	THR134
A	ARG272
A	ASP296
A	HIS321
A	ALA323
A	TRP324
A	HOH917
A	HOH925
A	ILE186
A	GLY187
A	GLY189
A	ARG190
A	THR191
A	TYR209
A	ASP210

site_id	AC2
Number of Residues	24
Details	BINDING SITE FOR RESIDUE NAD B 901

Chain	Residue
B	SER106
B	GLY107
B	THR134
B	ILE186
B	GLY187
B	GLY189
B	ARG190
B	THR191
B	TYR209
B	ASP210
B	PRO211
B	TYR212
B	HIS242
B	CYS243
B	ASN244
B	ASN246
B	ASN249
B	ALA270
B	ALA271
B	ARG272
B	ASP296
B	HIS321
B	ALA323
B	TRP324

site_id	AC3
Number of Residues	26
Details	BINDING SITE FOR RESIDUE NAD C 901

Chain	Residue
C	SER106
C	GLY107
C	THR134
C	ILE186
C	GLY187
C	GLY189
C	ARG190
C	THR191
C	TYR209
C	ASP210
C	PRO211
C	TYR212
C	LEU213
C	HIS242
C	CYS243
C	ASN244
C	ASN246
C	ASN249
C	ALA270
C	ALA271
C	ARG272
C	ASP296
C	ALA323
C	TRP324
C	HOH902
C	HOH903

site_id	AC4
Number of Residues	24
Details	BINDING SITE FOR RESIDUE NAD D 901

Chain	Residue
D	HOH906
D	SER106
D	THR134
D	GLY187
D	GLY189
D	ARG190
D	THR191
D	TYR209
D	ASP210
D	PRO211
D	TYR212
D	HIS242
D	CYS243
D	ASN244
D	ASN246
D	ASN249
D	ALA270
D	ALA271
D	ARG272
D	ASP296
D	VAL297
D	HIS321
D	ALA323
D	TRP324

site_id	AC5
Number of Residues	23
Details	BINDING SITE FOR RESIDUE NAD E 901

Chain	Residue
E	SER106
E	GLY107
E	THR134
E	GLY187
E	GLY189
E	ARG190
E	THR191
E	TYR209
E	ASP210
E	PRO211
E	TYR212
E	HIS242
E	CYS243
E	ASN244
E	ASN246
E	ASN249
E	ALA270
E	ALA271
E	ARG272
E	ASP296
E	HIS321
E	ALA323
E	TRP324

site_id	AC6
Number of Residues	25
Details	BINDING SITE FOR RESIDUE NAD F 901

Chain	Residue
F	SER106
F	GLY107
F	THR134
F	ILE186
F	GLY187
F	GLY189
F	ARG190
F	THR191
F	TYR209
F	ASP210
F	PRO211
F	TYR212
F	HIS242
F	CYS243
F	ASN244
F	ASN246
F	ASN249
F	ALA270
F	ALA271
F	ARG272
F	ASP296
F	HIS321
F	ALA323
F	TRP324
F	HOH910

site_id	AC7
Number of Residues	23
Details	BINDING SITE FOR RESIDUE NAD G 901

Chain	Residue
G	SER106
G	THR134
G	GLY187
G	GLY189
G	ARG190
G	THR191
G	TYR209
G	ASP210
G	PRO211
G	TYR212
G	HIS242
G	CYS243
G	ASN244
G	ASN246
G	ASN249
G	ALA270
G	ALA271
G	ARG272
G	ASP296
G	VAL297
G	HIS321
G	ALA323
G	TRP324

site_id	AC8
Number of Residues	25
Details	BINDING SITE FOR RESIDUE NAD H 901

Chain	Residue
H	SER106
H	THR134
H	ILE186
H	GLY187
H	GLY189
H	ARG190
H	THR191
H	TYR209
H	ASP210
H	PRO211
H	TYR212
H	LEU213
H	HIS242
H	CYS243
H	ASN244
H	ASN246
H	ASN249
H	ALA270
H	ALA271
H	ARG272
H	ASP296
H	ALA323
H	TRP324
H	HOH920
H	HOH927

Functional Information from PROSITE/UniProt

site_id	PS00671
Number of Residues	17
Details	D_2_HYDROXYACID_DH_3 D-isomer specific 2-hydroxyacid dehydrogenases signature 3. MRqGaFLVNaARGgLVD

Chain	Residue	Details
A	MET261-ASP277

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	16
Details	ACT_SITE: ACT_SITE => ECO:0000250

Chain	Residue	Details
A	ARG272
E	GLU301
F	ARG272
F	GLU301
G	ARG272
G	GLU301
H	ARG272
H	GLU301
A	GLU301
B	ARG272
B	GLU301
C	ARG272
C	GLU301
D	ARG272
D	GLU301
E	ARG272

site_id	SWS_FT_FI2
Number of Residues	8
Details	ACT_SITE: Proton donor => ECO:0000250

Chain	Residue	Details
A	HIS321
B	HIS321
C	HIS321
D	HIS321
E	HIS321
F	HIS321
G	HIS321
H	HIS321

site_id	SWS_FT_FI3
Number of Residues	8
Details	BINDING: BINDING => ECO:0000250

Chain	Residue	Details
A	SER106
B	SER106
C	SER106
D	SER106
E	SER106
F	SER106
G	SER106
H	SER106

site_id	SWS_FT_FI4
Number of Residues	48
Details	BINDING: BINDING => ECO:0000269\|Ref.20

Chain	Residue	Details
A	ILE186
B	ALA270
B	ASP296
B	HIS321
C	ILE186
C	ASP210
C	CYS243
C	ALA270
C	ASP296
C	HIS321
D	ILE186
A	ASP210
D	ASP210
D	CYS243
D	ALA270
D	ASP296
D	HIS321
E	ILE186
E	ASP210
E	CYS243
E	ALA270
E	ASP296
A	CYS243
E	HIS321
F	ILE186
F	ASP210
F	CYS243
F	ALA270
F	ASP296
F	HIS321
G	ILE186
G	ASP210
G	CYS243
A	ALA270
G	ALA270
G	ASP296
G	HIS321
H	ILE186
H	ASP210
H	CYS243
H	ALA270
H	ASP296
H	HIS321
A	ASP296
A	HIS321
B	ILE186
B	ASP210
B	CYS243

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)