Structure of PDB 3wfj Chain H

Receptor sequence
>3wfjH (length=250) Species: 1352 (Enterococcus faecium) [Search protein sequence]
IAIAGAGAMGSRFGLMLHQVLLIDGWAEHVLIILFTKAMQLEKMLQEVLC
LLNGIGHEDIIEKFVPMENIYIGNTMWTAGLEGPGQVGSGSVELQNLGDG
KEAAAKKLADKLNAHFSDNIHYSIYRKACVNGTMNGLCTILDVNMAELGK
TSTAHKMVATIVNEFAKVAAVEKIELDVPEVIAHCESCFDPETIGLHYPS
MYQDLIKNHRLTEIDYINGAISRKGKKYGVATPYCDFLTELVHAKEDSLN
3D structure
PDB3wfj The crystal structure of D-mandelate dehydrogenase reveals its distinct substrate and coenzyme recognition mechanisms from those of 2-ketopantoate reductase.
ChainH
Resolution2.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K187
Catalytic site (residue number reindexed from 1) K127
Enzyme Commision number 1.1.1.169: 2-dehydropantoate 2-reductase.
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 H G9 A10 M11 D30 W32 F77 T78 K79 Q82 L104 N105 W129 T130 A131 L133 R270 E273 G7 A8 M9 D24 W26 F35 T36 K37 Q40 L52 N53 W77 T78 A79 L81 R210 E213
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0008677 2-dehydropantoate 2-reductase activity
GO:0016491 oxidoreductase activity
GO:0050661 NADP binding
Biological Process
GO:0015940 pantothenate biosynthetic process
Cellular Component
GO:0005737 cytoplasm

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:3wfj, PDBe:3wfj, PDBj:3wfj
PDBsum3wfj
PubMed23954635
UniProtE3USM3

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