1RFV

Crystal structure of pyridoxal kinase complexed with ADP

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0005524	molecular_function	ATP binding
A	0005829	cellular_component	cytosol
A	0008478	molecular_function	pyridoxal kinase activity
A	0009443	biological_process	pyridoxal 5'-phosphate salvage
A	0016301	molecular_function	kinase activity
A	0016740	molecular_function	transferase activity
A	0042822	biological_process	pyridoxal phosphate metabolic process
A	0046872	molecular_function	metal ion binding
B	0000166	molecular_function	nucleotide binding
B	0005524	molecular_function	ATP binding
B	0005829	cellular_component	cytosol
B	0008478	molecular_function	pyridoxal kinase activity
B	0009443	biological_process	pyridoxal 5'-phosphate salvage
B	0016301	molecular_function	kinase activity
B	0016740	molecular_function	transferase activity
B	0042822	biological_process	pyridoxal phosphate metabolic process
B	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE ZN A 402

Chain	Residue
A	GLN119
A	ADP401

---

site_id	AC2
Number of Residues	1
Details	BINDING SITE FOR RESIDUE ZN B 1402

Chain	Residue
B	ADP1401

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site_id	AC3
Number of Residues	15
Details	BINDING SITE FOR RESIDUE ADP A 401

Chain	Residue
A	LYS225
A	VAL226
A	ALA228
A	THR233
A	PHE237
A	LEU267
A	ZN402
A	HOH404
A	HOH434
A	GLN119
A	ASN150
A	THR186
A	SER187
A	MET223
A	HIS224

---

site_id	AC4
Number of Residues	18
Details	BINDING SITE FOR RESIDUE ADP B 1401

Chain	Residue
B	ASP118
B	ASN150
B	THR186
B	SER187
B	MET223
B	HIS224
B	LYS225
B	VAL226
B	ALA228
B	THR233
B	PHE237
B	MET263
B	LEU267
B	ZN1402
B	HOH1403
B	HOH1414
B	HOH1421
B	HOH1440

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"O00764","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PubMed","id":"14722069","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1RFT","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PubMed","id":"12235162","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14722069","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1LHR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1RFT","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PubMed","id":"14722069","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1RFU","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"12235162","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14722069","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1LHR","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	10
Details	Binding site: {"evidences":[{"source":"PubMed","id":"12235162","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1LHR","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	8
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"O00764","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	4
Details	Annotated By Reference To The Literature 1tz3

Chain	Residue	Details
A	GLY234
A	THR233
A	GLY232
A	ASP235

---

site_id	CSA2
Number of Residues	4
Details	Annotated By Reference To The Literature 1tz3

Chain	Residue	Details
B	GLY234
B	THR233
B	GLY232
B	ASP235

---