Structure of PDB 4iym Chain J

Receptor sequence
>4iymJ (length=488) Species: 266834 (Sinorhizobium meliloti 1021) [Search protein sequence]
MYELGHFIDGKRVAGTSGRVSNIFNPATGEVQGTVALASDADLAAAVESA
KAAQPKWAATNPQRRARVFMKFVQLLNDNMNELAEMLSREHGKTIDDAKG
DIVRGLEVCEFVIGIPHLQKSEFTEGAGPGIDMYSIRQPVGIGAGITPFN
FPGMIPMWMFAPAIACGNAFILKPSERDPSVPIRLAELMIEAGLPAGILN
VVNGDKGAVDAILTHPDIAAVSFVGSTPIARYVYGTAAMNGKRAQCFGGA
KNHMIIMPDADLDQAANALIGAGYGSAGERCMAISVAVPVGEETANRLID
KLVPMVESLRIGPYTDEKADMGPVVTKEAEQRIRSLIDSGIEQGAKLVVD
GRDFKLQGYENGHFIGGCLFDDVTPDMDIYKTEIFGPVLSVVRARNYEEA
LSLPMKHEYGNGVAIYTRDGDAARDFASRINIGMVGVNVPIPVPLAYHSF
GGWKSSSFGDLNQHGTDSIKFWTRTKTITSRWPSGIKD
3D structure
PDB4iym Crystal structure of putative methylmalonate-semialdehyde dehydrogenase from Sinorhizobium meliloti 1021 complexed with NAD, target 011934
ChainJ
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) N148 K171 F245 C279 E381 Q461
Catalytic site (residue number reindexed from 1) N150 K173 F247 C281 E383 Q463
Enzyme Commision number 1.2.1.27: methylmalonate-semialdehyde dehydrogenase (CoA acylating).
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 J I144 T145 P146 F147 N148 F149 K171 E174 K204 F221 V222 G223 S224 I227 G246 C279 E381 F383 I146 T147 P148 F149 N150 F151 K173 E176 K206 F223 V224 G225 S226 I229 G248 C281 E383 F385
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0004491 methylmalonate-semialdehyde dehydrogenase (acylating, NAD) activity
GO:0016491 oxidoreductase activity
GO:0016620 oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
GO:0018478 malonate-semialdehyde dehydrogenase (acetylating) activity
Biological Process
GO:0006210 thymine catabolic process
GO:0006574 valine catabolic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:4iym, PDBe:4iym, PDBj:4iym
PDBsum4iym
PubMed
UniProtQ92RW4

[Back to BioLiP]