Structure of PDB 3giy Chain A

Receptor sequence
>3giyA (length=353) Species: 303 (Pseudomonas putida) [Search protein sequence]
NLFNVEDYRKLAQKRLPKMVYDYLEGGAEDEYGVKHNRDVFQQWRFKPKR
LVDVSRRSLQAEVLGKRQSMPLLIGPTALNGALWPKGDLALARAATKAGI
PFVLSTASNMSIEDLARQCDGDLWFQLYVIHREIAQGMVLKALHTGYTTL
VLTTDVAVNGYRERDLHNRFKIPPFLTLKNFEGIDLGKMDKANLEMQAAL
MSRQMDASFNWEALRWLRDLWPHKLLVKGLLSAEDADRCIAEGADGVILS
NHGGRQLDCAISPMEVLAQSVAKTGKPVLIDSGFRRGSDIVKALALGAEA
VLLGRATLYGLAARGETGVDEVLTLLKADIDRTLAQIGCPDITSLSPDYL
QNE
3D structure
PDB3giy Structures of the G81A mutant form of the active chimera of (S)-mandelate dehydrogenase and its complex with two of its substrates.
ChainA
Resolution1.6 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S108 Y131 T156 D158 K231 H255
Catalytic site (residue number reindexed from 1) S105 Y128 T153 D155 K228 H252
Enzyme Commision number 1.1.99.31: (S)-mandelate 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 FMN A Y26 P79 T80 A81 S108 Q129 Y131 T156 K231 H255 G256 R258 D284 S285 G286 R288 G307 R308 Y23 P76 T77 A78 S105 Q126 Y128 T153 K228 H252 G253 R255 D281 S282 G283 R285 G304 R305
Gene Ontology
Molecular Function
GO:0004459 L-lactate dehydrogenase activity
GO:0010181 FMN binding
GO:0016491 oxidoreductase activity
GO:0033720 (S)-mandelate dehydrogenase activity
Biological Process
GO:0009056 catabolic process
GO:0018924 mandelate metabolic process
GO:0019596 mandelate catabolic process
Cellular Component
GO:0005886 plasma membrane

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Cellular Component
External links
PDB RCSB:3giy, PDBe:3giy, PDBj:3giy
PDBsum3giy
PubMed19465768
UniProtP20932|MDLB_PSEPU (S)-mandelate dehydrogenase (Gene Name=mdlB)

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