2FPP

Crystal structure of pig GTP-specific succinyl-CoA synthetase from polyethylene glycol with chloride ions

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
B	0003824	molecular_function	catalytic activity
B	0004775	molecular_function	succinate-CoA ligase (ADP-forming) activity
B	0004776	molecular_function	succinate-CoA ligase (GDP-forming) activity
B	0005515	molecular_function	protein binding
B	0005524	molecular_function	ATP binding
B	0005525	molecular_function	GTP binding
B	0005737	cellular_component	cytoplasm
B	0005739	cellular_component	mitochondrion
B	0006099	biological_process	tricarboxylic acid cycle
B	0006104	biological_process	succinyl-CoA metabolic process
B	0016874	molecular_function	ligase activity
B	0042709	cellular_component	succinate-CoA ligase complex
B	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 A 307

Chain	Residue
A	ARG255
A	ARG256

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site_id	AC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 B 396

Chain	Residue
B	GLY53
B	ARG54

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site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 B 397

Chain	Residue
A	LYS53
B	LYS163
B	ASP164
B	SER165

---

site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL A 308

Chain	Residue
A	HOH354
B	LYS64
A	THR46

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Functional Information from PROSITE/UniProt

site_id	PS00399
Number of Residues	14
Details	SUCCINYL_COA_LIG_2 ATP-citrate lyase / succinyl-CoA ligases family active site. GltAppgr...RMGHAG

Chain	Residue	Details
A	GLY248-GLY261

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site_id	PS01216
Number of Residues	30
Details	SUCCINYL_COA_LIG_1 ATP-citrate lyase / succinyl-CoA ligases family signature 1. SRSGTLTyEavhqttqvglGqslcVGIGGD

Chain	Residue	Details
A	SER160-ASP189

---

site_id	PS01217
Number of Residues	26
Details	SUCCINYL_COA_LIG_3 ATP-citrate lyase / succinyl-CoA ligases family signature 3. GnIacFvNGAGLAmatcDiIflngGK

Chain	Residue	Details
B	GLY264-LYS289

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Tele-phosphohistidine intermediate => ECO:0000255|HAMAP-Rule:MF_03222, ECO:0000269|PubMed:10873456, ECO:0000269|PubMed:16481318

Chain	Residue	Details
A	NEP259
B	GLY53
B	LEU109

---

site_id	SWS_FT_FI2
Number of Residues	3
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03222, ECO:0000269|PubMed:26249701

Chain	Residue	Details
A	THR24
A	LYS50
A	ILE103

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03222, ECO:0000269|PubMed:27487822

Chain	Residue	Details
A	TYR167
B	GLY328

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P53597

Chain	Residue	Details
A	LYS14
B	ASP110

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9WUM5

Chain	Residue	Details
A	LYS17
A	LYS26
B	LYS102
B	LYS163
B	LYS234
B	LYS310
B	LYS349
B	LYS386

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q9WUM5

Chain	Residue	Details
A	LYS65
B	LYS301

---

site_id	SWS_FT_FI7
Number of Residues	1
Details	MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q9WUM5

Chain	Residue	Details
A	LYS298

---

site_id	SWS_FT_FI8
Number of Residues	2
Details	MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q96I99

Chain	Residue	Details
B	LYS190
B	LYS254

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	Annotated By Reference To The Literature 1cqj

Chain	Residue	Details
A	GLU217
B	GLU204
B	TYR116

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