4LCJ
CtBP2 in complex with substrate MTOB
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 | 25 |
Details | BINDING SITE FOR RESIDUE NAD A 401 |
Chain | Residue |
A | SER106 |
A | PRO211 |
A | TYR212 |
A | HIS242 |
A | CYS243 |
A | ASN244 |
A | ASN246 |
A | ASN249 |
A | ALA270 |
A | ALA271 |
A | ARG272 |
A | THR134 |
A | ASP296 |
A | HIS321 |
A | ALA323 |
A | TRP324 |
A | KMT402 |
A | HOH512 |
A | ILE186 |
A | GLY187 |
A | GLY189 |
A | ARG190 |
A | THR191 |
A | TYR209 |
A | ASP210 |
site_id | AC2 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE KMT A 402 |
Chain | Residue |
A | HIS83 |
A | ARG103 |
A | ILE104 |
A | GLY105 |
A | SER106 |
A | GLY107 |
A | ARG272 |
A | HIS321 |
A | TRP324 |
A | NAD401 |
site_id | AC3 |
Number of Residues | 26 |
Details | BINDING SITE FOR RESIDUE NAD B 401 |
Chain | Residue |
B | SER106 |
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 | VAL297 |
B | HIS321 |
B | ALA323 |
B | TRP324 |
B | KMT402 |
B | HOH528 |
site_id | AC4 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE KMT B 402 |
Chain | Residue |
B | TYR82 |
B | HIS83 |
B | ARG103 |
B | ILE104 |
B | GLY105 |
B | SER106 |
B | GLY107 |
B | ARG272 |
B | HIS321 |
B | TRP324 |
B | NAD401 |
site_id | AC5 |
Number of Residues | 26 |
Details | BINDING SITE FOR RESIDUE NAD C 401 |
Chain | Residue |
C | SER106 |
C | THR134 |
C | ILE186 |
C | GLY187 |
C | GLY189 |
C | ARG190 |
C | THR191 |
C | TYR209 |
C | ASP210 |
C | PRO211 |
C | TYR212 |
C | HIS242 |
C | CYS243 |
C | ASN244 |
C | ASN246 |
C | ASN249 |
C | ALA270 |
C | ALA271 |
C | ARG272 |
C | ASP296 |
C | VAL297 |
C | HIS321 |
C | ALA323 |
C | TRP324 |
C | KMT402 |
C | HOH514 |
site_id | AC6 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE KMT C 402 |
Chain | Residue |
C | ARG103 |
C | ILE104 |
C | GLY105 |
C | SER106 |
C | GLY107 |
C | ARG272 |
C | HIS321 |
C | NAD401 |
C | HIS83 |
site_id | AC7 |
Number of Residues | 23 |
Details | BINDING SITE FOR RESIDUE NAD D 401 |
Chain | Residue |
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 | HIS321 |
D | ALA323 |
D | TRP324 |
D | KMT402 |
site_id | AC8 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE KMT D 402 |
Chain | Residue |
D | HIS83 |
D | ARG103 |
D | ILE104 |
D | GLY105 |
D | SER106 |
D | GLY107 |
D | ARG272 |
D | HIS321 |
D | TRP324 |
D | NAD401 |
site_id | AC9 |
Number of Residues | 26 |
Details | BINDING SITE FOR RESIDUE NAD E 401 |
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 |
E | KMT402 |
E | HOH505 |
E | HOH515 |
site_id | BC1 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE KMT E 402 |
Chain | Residue |
E | HIS83 |
E | ARG103 |
E | ILE104 |
E | SER106 |
E | GLY107 |
E | ARG272 |
E | HIS321 |
E | TRP324 |
E | NAD401 |
site_id | BC2 |
Number of Residues | 25 |
Details | BINDING SITE FOR RESIDUE NAD F 401 |
Chain | Residue |
F | SER106 |
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 | ALA270 |
F | ALA271 |
F | ARG272 |
F | ASP296 |
F | VAL297 |
F | HIS321 |
F | ALA323 |
F | TRP324 |
F | KMT402 |
F | HOH508 |
site_id | BC3 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE KMT F 402 |
Chain | Residue |
F | HIS83 |
F | ARG103 |
F | ILE104 |
F | GLY105 |
F | SER106 |
F | GLY107 |
F | ARG272 |
F | HIS321 |
F | NAD401 |
site_id | BC4 |
Number of Residues | 25 |
Details | BINDING SITE FOR RESIDUE NAD G 401 |
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 | HIS321 |
G | ALA323 |
G | TRP324 |
G | KMT402 |
G | HOH505 |
G | HOH515 |
site_id | BC5 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE KMT G 402 |
Chain | Residue |
G | TYR82 |
G | HIS83 |
G | ILE104 |
G | GLY105 |
G | SER106 |
G | GLY107 |
G | ARG272 |
G | HIS321 |
G | TRP324 |
G | NAD401 |
site_id | BC6 |
Number of Residues | 25 |
Details | BINDING SITE FOR RESIDUE NAD H 401 |
Chain | Residue |
H | SER106 |
H | GLY107 |
H | THR134 |
H | GLY187 |
H | GLY189 |
H | ARG190 |
H | THR191 |
H | TYR209 |
H | ASP210 |
H | PRO211 |
H | TYR212 |
H | HIS242 |
H | CYS243 |
H | ASN244 |
H | ASN246 |
H | ASN249 |
H | ALA270 |
H | ALA271 |
H | ARG272 |
H | ASP296 |
H | HIS321 |
H | TRP324 |
H | KMT402 |
H | HOH520 |
H | HOH521 |
site_id | BC7 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE KMT H 402 |
Chain | Residue |
H | HIS83 |
H | ARG103 |
H | ILE104 |
H | GLY105 |
H | SER106 |
H | GLY107 |
H | ARG272 |
H | HIS321 |
H | NAD401 |
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 | |
A | GLU301 | |
B | ARG272 | |
B | GLU301 | |
C | ARG272 | |
C | GLU301 | |
D | ARG272 | |
D | GLU301 | |
E | ARG272 | |
E | GLU301 | |
F | ARG272 | |
F | GLU301 | |
G | ARG272 | |
G | GLU301 | |
H | ARG272 | |
H | GLU301 |
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 |
B | CYS243 | |
B | ALA270 | |
B | ASP296 | |
B | HIS321 | |
C | ILE186 | |
C | ASP210 | |
C | CYS243 | |
C | ALA270 | |
C | ASP296 | |
C | HIS321 | |
D | ILE186 | |
D | ASP210 | |
D | CYS243 | |
D | ALA270 | |
D | ASP296 | |
D | HIS321 | |
E | ILE186 | |
E | ASP210 | |
E | CYS243 | |
E | ALA270 | |
E | ASP296 | |
E | HIS321 | |
F | ILE186 | |
F | ASP210 | |
F | CYS243 | |
F | ALA270 | |
F | ASP296 | |
F | HIS321 | |
G | ILE186 | |
G | ASP210 | |
G | CYS243 | |
G | ALA270 | |
G | ASP296 | |
G | HIS321 | |
H | ILE186 | |
H | ASP210 | |
H | CYS243 | |
H | ALA270 | |
H | ASP296 | |
H | HIS321 | |
A | ILE186 | |
A | ASP210 | |
A | CYS243 | |
A | ALA270 | |
A | ASP296 | |
A | HIS321 | |
B | ILE186 | |
B | ASP210 |