Structure of PDB 2w2l Chain B

Receptor sequence
>2w2lB (length=345) Species: 29898 (Rhodotorula graminis) [Search protein sequence]
PRPRVLLLGDPARHLDDLWSDFQQKFEVIPANLTTHDGFKQALREKRYGD
FEAIIKLAVENGTESYPWNADLISHLPSSLKVFAAAGAGFDWLDLDALNE
RGVAFANSRGAGDTATSDLALYLILSVFRLASYSERAARTGDPETFNRVH
LEIGKSAHNPRGHVLGAVGLGAIQKEIARKAVHGLGMKLVYYDVAPADAE
TEKALGAERVDSLEELARRSDCVSVSVPYMKLTHHLIDEAFFAAMKPGSR
IVNTARGPVISQDALIAALKSGKLLSAGLDVHEFEPQVSKELIEMKHVTL
TTHIGGVAIETFHEFERLTMTNIDRFLLQGKPLLTPAGKVFAPSS
3D structure
PDB2w2l Crystal Structure of the Apo and Holo Forms of Rhodotorula Graminis D(-)-Mandelate Dehydrogenase
ChainB
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) G113 R257 D281 E286 H304
Catalytic site (residue number reindexed from 1) G112 R256 D280 E285 H303
Enzyme Commision number ?
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 G172 A173 I174 Y193 D194 V195 V228 P229 T255 A256 R257 H304 G306 G307 G171 A172 I173 Y192 D193 V194 V227 P228 T254 A255 R256 H303 G305 G306
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0016491 oxidoreductase activity
GO:0016616 oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
GO:0016618 hydroxypyruvate reductase [NAD(P)H] activity
GO:0030267 glyoxylate reductase (NADPH) activity
GO:0051287 NAD binding
Cellular Component
GO:0005829 cytosol

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Molecular Function
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Cellular Component
External links
PDB RCSB:2w2l, PDBe:2w2l, PDBj:2w2l
PDBsum2w2l
PubMed
UniProtQ7LLW9

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