Structure of PDB 6d97 Chain B

Receptor sequence
>6d97B (length=522) Species: 4577 (Zea mays) [Search protein sequence]
TPSFATVSPQEVSGSSPAEVQNFVQGSWTASANWNWIVDPLNGDKFIKVA
EVQGTEIKSFMESLSKCPKHGLHNPLKAPERYLMYGDISAKAAHMLGQPT
VLDFFAKLIQRVSPKSYQQALAEVQVSQKFLENFCGDQVRFLARSFAVPG
NHLGQRSNGYRWPYGPVAIITPFNFPLEIPLLQLMGALYMGNKPVLKVDS
KVSIVMEQMIRLLHDCGLPAEDMDFINSDGAVMNKLLLEANPKMTLFTGS
SRVAEKLAADLKGRVKLEDAGFDWKILGPDVQEVDYVAWVCDQDAYACSG
QKCSAQSVLFMHKNWSSSGLLEKMKKLSERRKLEDLTIGPVLTVTTEAMI
EHMNNLLKIRGSKVLFGGEPLANHSIPKIYGAMKPTAVFVPLEEILKSGN
FELVTKEIFGPFQVVTEYSEDQLELVLEACERMNAHLTAAIVSNDPLFLQ
DVLGRSVNGTTYAGIRARTTGAPQNHWFGPAGDPRGAGIGTPEAIKLVWS
CHREIIYDVGPVPESWALPSAT
3D structure
PDB6d97 Structural and Biochemical Characterization of Aldehyde Dehydrogenase 12, the Last Enzyme of Proline Catabolism in Plants.
ChainB
Resolution2.2 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 1.2.1.88: L-glutamate gamma-semialdehyde dehydrogenase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 NAD B I197 T198 P199 K224 D226 G257 M260 N261 F274 S277 V280 L284 I170 T171 P172 K197 D199 G230 M233 N234 F247 S250 V253 L257
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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