Structure of PDB 4ocp Chain A

Receptor sequence
>4ocpA (length=355) Species: 216816 (Bifidobacterium longum) [Search protein sequence]
ESNEVLFGIASHFALEGAVTGIEPYGDGHINTTYLVTTDGPRYILQQMNT
SIFPDTVNLMRNVELVTSTLKAQGKETLDIVPTTSGATWAEIDGGAWRVY
KFIEHTVSYNLVPNPDVFREAGSAFGDFQNFLSEFDASQLTETIAHFHDT
PHRFEDFKAALAADKLGRAAACQPEIDFYLSHADQYAVVMDGLRDGSIPL
RVTHNDTKLNNILMDATTGKARAIIDLDTIMPGSMLFDFGDSIRFGASTA
LEDEKDLSKVHFSTELFRAYTEGFVGELRGSITAREAELLPFSGNLLTME
CGMRFLADYLEGDIYFATKYPEHNLVRTRTQIKLVQEMEQKASETRAIVA
DIMEA
3D structure
PDB4ocp Insights into the binding specificity and catalytic mechanism of N-acetylhexosamine 1-phosphate kinases through multiple reaction complexes.
ChainA
Resolution1.938 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.7.1.162: N-acetylhexosamine 1-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 GN1 A H31 I32 F149 D208 K210 N213 D228 E254 C303 R306 Y317 H29 I30 F147 D206 K208 N211 D226 E252 C301 R304 Y315
BS02 ADP A G30 N33 I46 Q48 F104 I105 I227 D228 G28 N31 I44 Q46 F102 I103 I225 D226 PDBbind-CN: -logKd/Ki=6.10,Kd=0.8uM
BS03 MG A N213 D228 N211 D226
Gene Ontology
Molecular Function
GO:0004413 homoserine kinase activity
GO:0005524 ATP binding
GO:0016301 kinase activity
GO:0016773 phosphotransferase activity, alcohol group as acceptor
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0009088 threonine biosynthetic process
GO:0016310 phosphorylation

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:4ocp, PDBe:4ocp, PDBj:4ocp
PDBsum4ocp
PubMed24816108
UniProtE8MF12|NAHK_BIFL2 N-acetylhexosamine 1-kinase (Gene Name=nahK)

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