1EUC

CRYSTAL STRUCTURE OF DEPHOSPHORYLATED PIG HEART, GTP-SPECIFIC SUCCINYL-COA SYNTHETASE

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	10
Details	BINDING SITE FOR RESIDUE PO4 A 307

Chain	Residue
A	SER162
B	GLY274
A	GLY163
A	THR164
A	HIS259
A	HOH318
A	HOH325
A	HOH326
B	GLY272
B	ALA273

---

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 A 308

Chain	Residue
A	ARG255
A	ARG256
B	MET0
B	ASP227

---

site_id	AC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 B 396

Chain	Residue
B	GLY53
B	ARG54

---

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN B 400

Chain	Residue
B	CYS268
B	ALA276
B	CYS280
B	ASN292
B	HOH448

---

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

---

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	3
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03221, ECO:0000269|PubMed:16481318

Chain	Residue	Details
B	LYS36
B	LEU69
B	CYS125

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03221, ECO:0000305|PubMed:16481318

Chain	Residue	Details
B	LYS222
B	ILE236
A	LYS116

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03221, ECO:0000269|PubMed:27487822

Chain	Residue	Details
B	GLY287
B	ARG344

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	SITE: Important for substrate specificity => ECO:0000255|HAMAP-Rule:MF_03221

Chain	Residue	Details
B	VAL58
B	ASN126

---

site_id	SWS_FT_FI5
Number of Residues	7
Details	MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q9Z2I8

Chain	Residue	Details
B	GLY52
B	ILE111
B	ALA118
B	PRO179
B	ASN250
B	PHE326
B	GLN365

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q9Z2I8

Chain	Residue	Details
B	GLY57
B	LYS317

---

site_id	SWS_FT_FI7
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9Z2I8

Chain	Residue	Details
B	ILE140

---

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

Chain	Residue	Details
B	ASN206
B	VAL270

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1cqj

Chain	Residue	Details
A	HIS259
A	GLU217

---

site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1cqj

Chain	Residue	Details
B	GLU204
B	TYR116

---