2BTY

Acetylglutamate kinase from Thermotoga maritima complexed with its inhibitor arginine

Replaces:  1UVV

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003991	molecular_function	acetylglutamate kinase activity
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0006526	biological_process	L-arginine biosynthetic process
A	0016301	molecular_function	kinase activity
A	0016310	biological_process	phosphorylation
A	0042450	biological_process	arginine biosynthetic process via ornithine
B	0003991	molecular_function	acetylglutamate kinase activity
B	0005524	molecular_function	ATP binding
B	0005737	cellular_component	cytoplasm
B	0006526	biological_process	L-arginine biosynthetic process
B	0016301	molecular_function	kinase activity
B	0016310	biological_process	phosphorylation
B	0042450	biological_process	arginine biosynthetic process via ornithine
C	0003991	molecular_function	acetylglutamate kinase activity
C	0005524	molecular_function	ATP binding
C	0005737	cellular_component	cytoplasm
C	0006526	biological_process	L-arginine biosynthetic process
C	0016301	molecular_function	kinase activity
C	0016310	biological_process	phosphorylation
C	0042450	biological_process	arginine biosynthetic process via ornithine

Functional Information from PDB Data

site_id	AC1
Number of Residues	1
Details	BINDING SITE FOR RESIDUE K A1285

Chain	Residue
A	ASP160

---

site_id	AC2
Number of Residues	12
Details	BINDING SITE FOR RESIDUE ARG A1283

Chain	Residue
A	LYS271
A	GLY274
A	MET276
A	HOH2015
A	TYR15
A	PHE19
A	LYS196
A	SER214
A	GLU266
A	ILE267
A	SER269
A	ARG270

---

site_id	AC3
Number of Residues	13
Details	BINDING SITE FOR RESIDUE ARG B1283

Chain	Residue
B	TYR15
B	PHE19
B	LYS196
B	SER214
B	THR215
B	GLU266
B	ILE267
B	SER269
B	ARG270
B	LYS271
B	GLY274
B	MET276
B	HOH2015

---

site_id	AC4
Number of Residues	12
Details	BINDING SITE FOR RESIDUE ARG C1283

Chain	Residue
C	PHE19
C	LYS196
C	SER214
C	THR215
C	GLU266
C	ILE267
C	SER269
C	ARG270
C	LYS271
C	GLY272
C	GLY274
C	MET276

---

site_id	AC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE NLG A1284

Chain	Residue
A	LYS27
A	GLY29
A	GLY30
A	GLY61
A	GLY62
A	ASN180
A	ASP182

---

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NLG B1284

Chain	Residue
B	LYS27
B	GLY29
B	GLY30
B	GLY61
B	ASN180
B	ASP182

---

site_id	AC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE NLG C1284

Chain	Residue
C	LYS27
C	GLY30
C	GLY61
C	GLY62
C	GLY63
C	ILE179
C	ASN180

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00082

Chain	Residue	Details
A	GLY62
A	ARG84
B	GLY62
B	ARG84
C	GLY62
C	ARG84

---

site_id	SWS_FT_FI2
Number of Residues	3
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00082, ECO:0000269|PubMed:16376937

Chain	Residue	Details
A	ASN178
B	ASN178
C	ASN178

---

site_id	SWS_FT_FI3
Number of Residues	9
Details	BINDING: BINDING => ECO:0000269|PubMed:16376937, ECO:0007744|PDB:2BTY

Chain	Residue	Details
A	LYS196
A	SER214
A	GLU266
B	LYS196
B	SER214
B	GLU266
C	LYS196
C	SER214
C	GLU266

---

site_id	SWS_FT_FI4
Number of Residues	6
Details	SITE: Transition state stabilizer => ECO:0000255|HAMAP-Rule:MF_00082

Chain	Residue	Details
A	LYS27
A	LYS237
B	LYS27
B	LYS237
C	LYS27
C	LYS237

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	4
Details	Annotated By Reference To The Literature 1oh9

Chain	Residue	Details
A	LYS237
A	GLY30
A	GLY63
A	LYS27

---

site_id	CSA2
Number of Residues	4
Details	Annotated By Reference To The Literature 1oh9

Chain	Residue	Details
B	LYS237
B	GLY30
B	GLY63
B	LYS27

---

site_id	CSA3
Number of Residues	4
Details	Annotated By Reference To The Literature 1oh9

Chain	Residue	Details
C	LYS237
C	GLY30
C	GLY63
C	LYS27

---