Structure of PDB 5c3z Chain A

Receptor sequence
>5c3zA (length=316) Species: 9606 (Homo sapiens) [Search protein sequence]
WQEEVAAVVVVGSCMTDLVSLTSRLPKTGETIHGHKFFIGFGGKGANQCV
QAARLGAMTSMVCKVGKDSFGNDYIENLKQNDISTEFTYQTKDAATGTAS
IIVNNEGQNIIVIVAGANLLLNTEDLRAAANVISRAKVMVCQLEITPATS
LEALTMARRSGVKTLFNPAPAIADLDPQFYTLSDVFCCNESEAEILTGLT
VGSAADAGEAALVLLKRGCQVVIITLGAEGCVVLSQTEPEPKHIPTEKVK
AVDTTGAGDSFVGALAFYLAYYPNLSLEDMLNRSNFIAAVSVQAAGTQSS
YPYKKDLPLTLFLEHH
3D structure
PDB5c3z Crystal structure of human ribokinase in complex with AMPPCP in C2 spacegroup
ChainA
Resolution1.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) G266 A267 G268 D269
Catalytic site (residue number reindexed from 1) G256 A257 G258 D259
Enzyme Commision number 2.7.1.15: ribokinase.
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 A N199 T235 G237 A238 G240 V259 T264 A267 G268 N295 A298 N189 T225 G227 A228 G230 V249 T254 A257 G258 N285 A288
Gene Ontology
Molecular Function
GO:0004747 ribokinase activity
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0016301 kinase activity
GO:0042802 identical protein binding
GO:0046872 metal ion binding
Biological Process
GO:0006014 D-ribose metabolic process
GO:0006098 pentose-phosphate shunt
GO:0006753 nucleoside phosphate metabolic process
GO:0016310 phosphorylation
GO:0019303 D-ribose catabolic process
GO:0046835 carbohydrate phosphorylation
Cellular Component
GO:0005634 nucleus
GO:0005737 cytoplasm
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5c3z, PDBe:5c3z, PDBj:5c3z
PDBsum5c3z
PubMed
UniProtQ9H477|RBSK_HUMAN Ribokinase (Gene Name=RBKS)

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