Structure of PDB 6d97 Chain B Binding Site BS01

Receptor Information
>6d97 Chain B (length=522) Species: 4577 (Zea mays) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
TPSFATVSPQEVSGSSPAEVQNFVQGSWTASANWNWIVDPLNGDKFIKVA
EVQGTEIKSFMESLSKCPKHGLHNPLKAPERYLMYGDISAKAAHMLGQPT
VLDFFAKLIQRVSPKSYQQALAEVQVSQKFLENFCGDQVRFLARSFAVPG
NHLGQRSNGYRWPYGPVAIITPFNFPLEIPLLQLMGALYMGNKPVLKVDS
KVSIVMEQMIRLLHDCGLPAEDMDFINSDGAVMNKLLLEANPKMTLFTGS
SRVAEKLAADLKGRVKLEDAGFDWKILGPDVQEVDYVAWVCDQDAYACSG
QKCSAQSVLFMHKNWSSSGLLEKMKKLSERRKLEDLTIGPVLTVTTEAMI
EHMNNLLKIRGSKVLFGGEPLANHSIPKIYGAMKPTAVFVPLEEILKSGN
FELVTKEIFGPFQVVTEYSEDQLELVLEACERMNAHLTAAIVSNDPLFLQ
DVLGRSVNGTTYAGIRARTTGAPQNHWFGPAGDPRGAGIGTPEAIKLVWS
CHREIIYDVGPVPESWALPSAT
Ligand information
Ligand IDNAD
InChIInChI=1S/C21H27N7O14P2/c22-17-12-19(25-7-24-17)28(8-26-12)21-16(32)14(30)11(41-21)6-39-44(36,37)42-43(34,35)38-5-10-13(29)15(31)20(40-10)27-3-1-2-9(4-27)18(23)33/h1-4,7-8,10-11,13-16,20-21,29-32H,5-6H2,(H5-,22,23,24,25,33,34,35,36,37)/t10-,11-,13-,14-,15-,16-,20-,21-/m1/s1
InChIKeyBAWFJGJZGIEFAR-NNYOXOHSSA-N
SMILES
SoftwareSMILES
CACTVS 3.341NC(=O)c1ccc[n+](c1)[C@@H]2O[C@H](CO[P]([O-])(=O)O[P@](O)(=O)OC[C@H]3O[C@H]([C@H](O)[C@@H]3O)n4cnc5c(N)ncnc45)[C@@H](O)[C@H]2O
OpenEye OEToolkits 1.5.0c1cc(c[n+](c1)C2C(C(C(O2)COP(=O)([O-])OP(=O)(O)OCC3C(C(C(O3)n4cnc5c4ncnc5N)O)O)O)O)C(=O)N
CACTVS 3.341NC(=O)c1ccc[n+](c1)[CH]2O[CH](CO[P]([O-])(=O)O[P](O)(=O)OC[CH]3O[CH]([CH](O)[CH]3O)n4cnc5c(N)ncnc45)[CH](O)[CH]2O
OpenEye OEToolkits 1.5.0c1cc(c[n+](c1)[C@H]2[C@@H]([C@@H]([C@H](O2)CO[P@@](=O)([O-])O[P@@](=O)(O)OC[C@@H]3[C@H]([C@H]([C@@H](O3)n4cnc5c4ncnc5N)O)O)O)O)C(=O)N
FormulaC21 H27 N7 O14 P2
NameNICOTINAMIDE-ADENINE-DINUCLEOTIDE
ChEMBLCHEMBL1234613
DrugBankDB14128
ZINC
PDB chain6d97 Chain B Residue 601 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB6d97 Structural and Biochemical Characterization of Aldehyde Dehydrogenase 12, the Last Enzyme of Proline Catabolism in Plants.
Resolution2.2 Å
Binding residue
(original residue number in PDB)		I197 T198 P199 K224 D226 G257 M260 N261 F274 S277 V280 L284
Binding residue
(residue number reindexed from 1)		I170 T171 P172 K197 D199 G230 M233 N234 F247 S250 V253 L257
Annotation score4
Enzymatic activity
Enzyme Commision number 1.2.1.88: L-glutamate gamma-semialdehyde dehydrogenase.
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0003842 1-pyrroline-5-carboxylate dehydrogenase activity
GO:0004029 aldehyde dehydrogenase (NAD+) activity
GO:0016491 oxidoreductase activity
GO:0016620 oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor

View graph for
Molecular Function
External links
PDB RCSB:6d97, PDBe:6d97, PDBj:6d97
PDBsum6d97
PubMed30580036
UniProtA0A2H4PMI3

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