Structure of PDB 5x20 Chain C

Receptor sequence
>5x20C (length=312) Species: 333849 (Enterococcus faecium DO) [Search protein sequence]
MKIAIAGAGAMGSRFGLMLHQSGNEVLLIDGWAEHVQQIKEHGLQANFNG
KEVEAKLPIVLQSEVEKEDQVDLIILFTKAMQLEKMLQDIQSLIKKDTEV
LCLLNGIGHEDIIEKFVPMENIYIGNTMWTAGLEGPGQVKLFGSGSVELQ
NLGDGKEAAAKKLADKLSESGLNAHFSDNIHYSIYRKACVNGTMNGLCTI
LDVNMAELGKTSTAHKMVATIVNEFAKVAAVEKIELDVPEVIAHCESCFD
PETIGLHYPSMYQDLIKNHRLTEIDYINGAISRKGKKYGVATPYCDFLTE
LVHAKEDSLNVK
3D structure
PDB5x20 The ternary complex structure of d-mandelate dehydrogenase with NADH and anilino(oxo)acetate.
ChainC
Resolution2.4 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) K187
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 C G9 A10 M11 D30 W32 T78 K79 Q82 L104 N105 W129 T130 A131 L133 R270 E273 G9 A10 M11 D30 W32 T78 K79 Q82 L104 N105 W129 T130 A131 L133 R270 E273
BS02 AOT C N105 M128 K187 N191 I254 S260 N105 M128 K187 N191 I254 S260
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:5x20, PDBe:5x20, PDBj:5x20
PDBsum5x20
PubMed28327357
UniProtQ3Y316

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