Structure of PDB 1eyy Chain D

Receptor sequence
>1eyyD (length=502) Species: 669 (Vibrio harveyi) [Search protein sequence]
NVFYATNAFTGEALPLAFPVHTEVEVNQAATAAAKVARDFRRLNNSKRAS
LLRTIASELEARSDDIIARAHLETALPEVRLTGEIARTANQLRLFADVVN
SGSYHQAILDTPNPTRAPLPKPDIRRQQIALGPVAVFGASNFPLAFSAAG
GDTASALAAGCPVIVKGHTAHPGTSQIVAECIEQALKQEQLPQAIFTLLQ
GNQRALGQALVSHPEIKAVGFTGSVGGGRALFNLAHERPEPIPFYGELGA
INPTFIFPSAMRAKADLADQFVASMTMGCGQFCTKPGVVFALNTPETQAF
IETAQSLIRQQSPSTLLTPGIRDSYQSQVVSRGSDDGIDVTFSQAESPCV
ASALFVTSSENWRKHPAWEEEIFGPQSLIVVCENVADMLSLSEMLAGSLT
ATIHATEEDYPQVSQLIPRLEEIAGRLVFNGWPTGVEVGYAMVHGGPYPA
STHSASTSVGAEAIHRWLRPVAYQALPESLLPDSLKAENPLEIARAVDGK
AA
3D structure
PDB1eyy Crystal structure of the NADP+-dependent aldehyde dehydrogenase from Vibrio harveyi: structural implications for cofactor specificity and affinity.
ChainD
Resolution2.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) N147 E253 C289
Catalytic site (residue number reindexed from 1) N141 E247 C283
Enzyme Commision number 1.2.1.4: aldehyde dehydrogenase (NADP(+)).
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 NAP D S146 K172 H174 T175 R210 F227 S230 S140 K166 H168 T169 R204 F221 S224
Gene Ontology
Molecular Function
GO:0016491 oxidoreductase activity
GO:0016620 oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
GO:0033721 aldehyde dehydrogenase (NADP+) activity

View graph for
Molecular Function
External links
PDB RCSB:1eyy, PDBe:1eyy, PDBj:1eyy
PDBsum1eyy
PubMed10903148
UniProtQ56694|ALDH_VIBHA NADP-dependent fatty aldehyde dehydrogenase (Gene Name=aldH)

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