1LHR

Crystal Structure of Pyridoxal Kinase complexed with ATP

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
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	0042816	biological_process	vitamin B6 metabolic process
A	0046872	molecular_function	metal ion binding
B	0005524	molecular_function	ATP binding
B	0005737	cellular_component	cytoplasm
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	0042816	biological_process	vitamin B6 metabolic process
B	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE ZN A 403

Chain	Residue
A	GLN119
A	ATP401
A	K405

---

site_id	AC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE ZN B 404

Chain	Residue
B	ATP402
B	K406

---

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE K A 405

Chain	Residue
A	ATP401
A	ZN403
A	ASP113
A	THR148
A	GLU153
A	THR186

---

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE K B 406

Chain	Residue
B	ASP113
B	THR148
B	THR186
B	ATP402
B	ZN404
B	HOH418

---

site_id	AC5
Number of Residues	16
Details	BINDING SITE FOR RESIDUE ATP A 401

Chain	Residue
A	GLN119
A	ASN150
A	THR186
A	SER187
A	MET223
A	HIS224
A	LYS225
A	VAL226
A	ALA228
A	THR233
A	GLY234
A	PHE237
A	LEU267
A	ZN403
A	K405
A	HOH420

---

site_id	AC6
Number of Residues	20
Details	BINDING SITE FOR RESIDUE ATP B 402

Chain	Residue
B	ASP118
B	TYR127
B	ASN150
B	THR186
B	SER187
B	MET223
B	HIS224
B	LYS225
B	VAL226
B	THR233
B	GLY234
B	PHE237
B	MET263
B	LEU267
B	ZN404
B	K406
B	HOH439
B	HOH440
B	HOH455
B	HOH458

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:O00764

Chain	Residue	Details
A	ASP235
B	ASP235

---

site_id	SWS_FT_FI2
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269|PubMed:14722069, ECO:0007744|PDB:1RFT

Chain	Residue	Details
A	SER12
A	THR47
A	ASP235
B	SER12
B	THR47
B	ASP235

---

site_id	SWS_FT_FI3
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269|PubMed:12235162, ECO:0000269|PubMed:14722069, ECO:0007744|PDB:1LHR, ECO:0007744|PDB:1RFT

Chain	Residue	Details
A	ASP113
A	THR148
A	THR186
B	ASP113
B	THR148
B	THR186

---

site_id	SWS_FT_FI4
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|PubMed:14722069, ECO:0007744|PDB:1RFU

Chain	Residue	Details
A	TYR127
A	GLY232
B	TYR127
B	GLY232

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:12235162, ECO:0000269|PubMed:14722069, ECO:0007744|PDB:1LHR

Chain	Residue	Details
A	ASN150
B	ASN150

---

site_id	SWS_FT_FI6
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|PubMed:12235162, ECO:0007744|PDB:1LHR

Chain	Residue	Details
A	MET223
A	THR233
B	MET223
B	THR233

---

site_id	SWS_FT_FI7
Number of Residues	2
Details	MOD_RES: N-acetylmethionine => ECO:0000269|PubMed:10395444

Chain	Residue	Details
A	MET1
B	MET1

---

site_id	SWS_FT_FI8
Number of Residues	8
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:O00764

Chain	Residue	Details
A	SER59
A	SER164
A	SER213
A	SER285
B	SER59
B	SER164
B	SER213
B	SER285

---

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

---