BioLiP

Structure of PDB 4c5m Chain C

Receptor sequence

>4c5mC (length=273) Species: 158878 (Staphylococcus aureus subsp. aureus Mu50) [Search protein sequence]

GALKKVLTIAGSDTSAGAGMQADLKTFQELDTYGMVALTAIVTMDKDTWS
HDVTPLPMDVFEKQLETALSIGPDAIKTGMLGTEEIIKRAGEVYEASNAQ
YFVVDPVMVCDEVLNPGNTEAMIKYLLPKATVVTPNLFEAGQLSGLGKLN
SIEDMKKAATIIFDKGAQHVIIKGGKALDQDKSYDLYYDGQTFYQLTTDM
FQQSYNHGAGCTFAAATTAYLANGKSPKEAVISAKAFVASAIKNGWKMND
FVGPVDHGAYNRIEHIDVEVTEV

3D structure

PDB

4c5m A Subfamily of Bacterial Ribokinases Utilizes a Hemithioacetal for Pyridoxal Phosphate Salvage.

Chain

Resolution

1.45 Å

3D
structure

Catalytic site residues are labeled in the structure
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Enzymatic activity

Catalytic site (original residue number in PDB)	K176 N209 G211 A212 G213 C214
Catalytic site (residue number reindexed from 1)	K173 N206 G208 A209 G210 C211
Enzyme Commision number	2.7.1.35: pyridoxal kinase.

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	ACP	C	K176 K179 S186 D188 M203 F204 N209 I245	K173 K176 S183 D185 M200 F201 N206 I242

Gene Ontology

	Molecular Function
GO:0000166	nucleotide binding
GO:0008902	hydroxymethylpyrimidine kinase activity
GO:0008972	phosphomethylpyrimidine kinase activity
GO:0016301	kinase activity

	Biological Process
GO:0009228	thiamine biosynthetic process
GO:0016310	phosphorylation

	Cellular Component
GO:0005829	cytosol

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Molecular Function

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Biological Process

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Cellular Component

PDB	RCSB:4c5m, PDBe:4c5m, PDBj:4c5m
PDBsum	4c5m
PubMed	24601602
UniProt	A0A0H3JTP0