Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2SCU

A detailed description of the structure of Succinyl-COA synthetase from Escherichia coli

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0003824	molecular_function	catalytic activity
A	0004775	molecular_function	succinate-CoA ligase (ADP-forming) activity
A	0004776	molecular_function	succinate-CoA ligase (GDP-forming) activity
A	0005515	molecular_function	protein binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006099	biological_process	tricarboxylic acid cycle
A	0009361	cellular_component	succinate-CoA ligase complex (ADP-forming)
A	0016874	molecular_function	ligase activity
B	0000166	molecular_function	nucleotide binding
B	0000287	molecular_function	magnesium ion binding
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	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006099	biological_process	tricarboxylic acid cycle
B	0006104	biological_process	succinyl-CoA metabolic process
B	0009361	cellular_component	succinate-CoA ligase complex (ADP-forming)
B	0016874	molecular_function	ligase activity
B	0042709	cellular_component	succinate-CoA ligase complex
B	0046872	molecular_function	metal ion binding
D	0000166	molecular_function	nucleotide binding
D	0003824	molecular_function	catalytic activity
D	0004775	molecular_function	succinate-CoA ligase (ADP-forming) activity
D	0004776	molecular_function	succinate-CoA ligase (GDP-forming) activity
D	0005515	molecular_function	protein binding
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0006099	biological_process	tricarboxylic acid cycle
D	0009361	cellular_component	succinate-CoA ligase complex (ADP-forming)
D	0016874	molecular_function	ligase activity
E	0000166	molecular_function	nucleotide binding
E	0000287	molecular_function	magnesium ion binding
E	0003824	molecular_function	catalytic activity
E	0004775	molecular_function	succinate-CoA ligase (ADP-forming) activity
E	0004776	molecular_function	succinate-CoA ligase (GDP-forming) activity
E	0005515	molecular_function	protein binding
E	0005524	molecular_function	ATP binding
E	0005737	cellular_component	cytoplasm
E	0005829	cellular_component	cytosol
E	0006099	biological_process	tricarboxylic acid cycle
E	0006104	biological_process	succinyl-CoA metabolic process
E	0009361	cellular_component	succinate-CoA ligase complex (ADP-forming)
E	0016874	molecular_function	ligase activity
E	0042709	cellular_component	succinate-CoA ligase complex
E	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 B 400

Chain	Residue
B	GLY53
B	ARG54
B	GLY55
B	ASP213

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 E 401

Chain	Residue
E	GLY53
E	ARG54
E	GLY55
E	ASP213
E	HOH1365

site_id	AC3
Number of Residues	29
Details	BINDING SITE FOR RESIDUE COA A 300

Chain	Residue
A	GLY14
A	THR16
A	GLY17
A	SER18
A	GLN19
A	VAL38
A	PRO40
A	LYS42
A	TYR71
A	VAL72
A	PRO73
A	ILE95
A	THR96
A	GLU97
A	ASN122
A	CYS123
A	PRO124
A	HOH1005
A	HOH1006
A	HOH1010
A	HOH1031
A	HOH1350
A	HOH1355
A	HOH1483
B	HOH1173
E	ARG29
E	GLU33
E	SER36
E	LYS66

site_id	AC4
Number of Residues	30
Details	BINDING SITE FOR RESIDUE COA D 301

Chain	Residue
B	ARG29
B	GLU33
B	SER36
B	LYS66
B	HOH1122
D	GLY14
D	THR16
D	GLY17
D	SER18
D	GLN19
D	VAL38
D	PRO40
D	LYS42
D	TYR71
D	VAL72
D	SER80
D	ILE95
D	THR96
D	GLU97
D	ASN122
D	CYS123
D	NEP246
D	HOH1119
D	HOH1253
D	HOH1254
D	HOH1255
D	HOH1273
D	HOH1277
D	HOH1476
D	HOH1485

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
B	GLY257-GLU282

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

Chain	Residue	Details
A	GLY235-GLY248

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

Chain	Residue	Details
A	SER151-ASP180

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	14
Details	BINDING: BINDING => ECO:0000255\|HAMAP-Rule:MF_00558, ECO:0000269\|PubMed:10625475

Chain	Residue	Details
B	LYS46
E	GLU99
E	THR102
E	GLU107
E	ASN199
E	ASP213
B	GLY53
B	GLU99
B	THR102
B	GLU107
B	ASN199
B	ASP213
E	LYS46
E	GLY53

site_id	SWS_FT_FI2
Number of Residues	4
Details	BINDING: BINDING => ECO:0000255\|HAMAP-Rule:MF_00558

Chain	Residue	Details
B	ASN264
B	GLY321
E	ASN264
E	GLY321
D	LYS42
D	ILE95

site_id	SWS_FT_FI3
Number of Residues	2
Details	BINDING: BINDING => ECO:0000255\|HAMAP-Rule:MF_01988

Chain	Residue	Details
A	TYR158
D	TYR158

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	2
Details	M-CSA 476

Chain	Residue	Details
B	TYR109	electrostatic stabiliser, steric role
B	GLU197	electrostatic stabiliser, modifies pKa

site_id	MCSA2
Number of Residues	2
Details	M-CSA 476

Chain	Residue	Details
E	TYR109	electrostatic stabiliser, steric role
E	GLU197	electrostatic stabiliser, modifies pKa

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)