6WK0

Crystal structure of human ribokinase in complex with AMPPCP and ribose

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0004747	molecular_function	ribokinase activity
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005634	cellular_component	nucleus
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006014	biological_process	D-ribose metabolic process
A	0006098	biological_process	pentose-phosphate shunt
A	0016301	molecular_function	kinase activity
A	0016740	molecular_function	transferase activity
A	0019303	biological_process	D-ribose catabolic process
A	0042802	molecular_function	identical protein binding
A	0046835	biological_process	carbohydrate phosphorylation
A	0046872	molecular_function	metal ion binding
B	0000166	molecular_function	nucleotide binding
B	0004747	molecular_function	ribokinase activity
B	0005515	molecular_function	protein binding
B	0005524	molecular_function	ATP binding
B	0005634	cellular_component	nucleus
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006014	biological_process	D-ribose metabolic process
B	0006098	biological_process	pentose-phosphate shunt
B	0016301	molecular_function	kinase activity
B	0016740	molecular_function	transferase activity
B	0019303	biological_process	D-ribose catabolic process
B	0042802	molecular_function	identical protein binding
B	0046835	biological_process	carbohydrate phosphorylation
B	0046872	molecular_function	metal ion binding
C	0000166	molecular_function	nucleotide binding
C	0004747	molecular_function	ribokinase activity
C	0005515	molecular_function	protein binding
C	0005524	molecular_function	ATP binding
C	0005634	cellular_component	nucleus
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0006014	biological_process	D-ribose metabolic process
C	0006098	biological_process	pentose-phosphate shunt
C	0016301	molecular_function	kinase activity
C	0016740	molecular_function	transferase activity
C	0019303	biological_process	D-ribose catabolic process
C	0042802	molecular_function	identical protein binding
C	0046835	biological_process	carbohydrate phosphorylation
C	0046872	molecular_function	metal ion binding
D	0000166	molecular_function	nucleotide binding
D	0004747	molecular_function	ribokinase activity
D	0005515	molecular_function	protein binding
D	0005524	molecular_function	ATP binding
D	0005634	cellular_component	nucleus
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0006014	biological_process	D-ribose metabolic process
D	0006098	biological_process	pentose-phosphate shunt
D	0016301	molecular_function	kinase activity
D	0016740	molecular_function	transferase activity
D	0019303	biological_process	D-ribose catabolic process
D	0042802	molecular_function	identical protein binding
D	0046835	biological_process	carbohydrate phosphorylation
D	0046872	molecular_function	metal ion binding

Functional Information from PROSITE/UniProt

site_id	PS00584
Number of Residues	14
Details	PFKB_KINASES_2 pfkB family of carbohydrate kinases signature 2. DTtGAGDsfvGALA

Chain	Residue	Details
A	ASP263-ALA276

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"P0A9J6","evidenceCode":"ECO:0000250"},{"source":"HAMAP-Rule","id":"MF_03215","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	40
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P0A9J6","evidenceCode":"ECO:0000250"},{"source":"HAMAP-Rule","id":"MF_03215","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	36
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03215","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JAN-2006","submissionDatabase":"PDB data bank","title":"Crystal structure of human ribokinase.","authoringGroup":["Structural genomics consortium (SGC)"]}}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	16
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03215","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000305","citation":{"citationType":"submission","publicationDate":"JAN-2006","submissionDatabase":"PDB data bank","title":"Crystal structure of human ribokinase.","authoringGroup":["Structural genomics consortium (SGC)"]}}]}

Chain

Residue

Details

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