Structure of PDB 1ez0 Chain C

Receptor sequence
>1ez0C (length=502) Species: 669 (Vibrio harveyi) [Search protein sequence]
NVFYATNAFTGEALPLAFPVHTEVEVNQAATAAAKVARDFRRLNNSKRAS
LLRTIASELEARSDDIIARAHLETALPEVRLTGEIARTANQLRLFADVVN
SGSYHQAILDTPNPTRAPLPKPDIRRQQIALGPVAVFGASNFPLAFSAAG
GDTASALAAGCPVIVKGHTAHPGTSQIVAECIEQALKQEQLPQAIFTLLQ
GNQRALGQALVSHPEIKAVGFTGSVGGGRALFNLAHERPEPIPFYGELGA
INPTFIFPSAMRAKADLADQFVASMTMGCGQFCTKPGVVFALNTPETQAF
IETAQSLIRQQSPSTLLTPGIRDSYQSQVVSRGSDDGIDVTFSQAESPCV
ASALFVTSSENWRKHPAWEEEIFGPQSLIVVCENVADMLSLSEMLAGSLT
ATIHATEEDYPQVSQLIPRLEEIAGRLVFNGWPTGVEVGYAMVHGGPYPA
STHSASTSVGAEAIHRWLRPVAYQALPESLLPDSLKAENPLEIARAVDGK
AA
3D structure
PDB1ez0 Crystal structure of the NADP+-dependent aldehyde dehydrogenase from Vibrio harveyi: structural implications for cofactor specificity and affinity.
ChainC
Resolution2.1 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 C S146 N147 K172 H174 T175 R210 Q214 F227 T228 G229 S230 E253 C289 F379 L405 H450 S140 N141 K166 H168 T169 R204 Q208 F221 T222 G223 S224 E247 C283 F373 L399 H444
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:1ez0, PDBe:1ez0, PDBj:1ez0
PDBsum1ez0
PubMed10903148
UniProtQ56694|ALDH_VIBHA NADP-dependent fatty aldehyde dehydrogenase (Gene Name=aldH)

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