Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1CQI

Crystal Structure of the Complex of ADP and MG2+ with Dephosphorylated E. Coli Succinyl-CoA Synthetase

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
A	0042709	cellular_component	succinate-CoA ligase complex
A	0046777	biological_process	protein autophosphorylation
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
D	0042709	cellular_component	succinate-CoA ligase complex
D	0046777	biological_process	protein autophosphorylation
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	3
Details	BINDING SITE FOR RESIDUE MG B 501

Chain	Residue
B	ASN199
B	ASP213
B	ADP801

site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG E 502

Chain	Residue
E	ASN199
E	ASP213
E	ADP802

site_id	AC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PO4 A 601

Chain	Residue
A	HIS246
B	GLY265
B	ALA266
B	GLY267
A	SER153
A	GLY154
A	THR155

site_id	AC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PO4 D 602

Chain	Residue
D	SER153
D	GLY154
D	THR155
D	HIS246
E	GLY265
E	ALA266
E	GLY267

site_id	AC5
Number of Residues	20
Details	BINDING SITE FOR RESIDUE COA A 701

Chain	Residue
A	GLY14
A	THR16
A	GLY17
A	SER18
A	GLN19
A	PRO40
A	LYS42
A	TYR71
A	VAL72
A	PRO73
A	ILE95
A	THR96
A	GLU97
A	CYS123
A	ILE136
B	ARG161
E	ARG29
E	GLU33
E	SER36
E	LYS66

site_id	AC6
Number of Residues	19
Details	BINDING SITE FOR RESIDUE COA D 702

Chain	Residue
B	ARG29
B	GLU33
B	SER36
B	LYS66
D	GLY14
D	THR16
D	GLY17
D	SER18
D	GLN19
D	PRO40
D	LYS42
D	TYR71
D	VAL72
D	PRO73
D	ILE95
D	THR96
D	GLU97
D	CYS123
D	ILE136

site_id	AC7
Number of Residues	15
Details	BINDING SITE FOR RESIDUE ADP B 801

Chain	Residue
B	VAL44
B	LYS46
B	GLY53
B	ARG54
B	GLY55
B	GLU99
B	ALA100
B	ALA101
B	THR102
B	GLU107
B	ASN199
B	PRO200
B	LEU212
B	ASP213
B	MG501

site_id	AC8
Number of Residues	15
Details	BINDING SITE FOR RESIDUE ADP E 802

Chain	Residue
E	VAL44
E	LYS46
E	GLY53
E	ARG54
E	GLY55
E	GLU99
E	ALA100
E	ALA101
E	THR102
E	GLU107
E	ASN199
E	PRO200
E	LEU212
E	ASP213
E	MG502

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. 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

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

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Active site: {"description":"Tele-phosphohistidine intermediate","evidences":[{"source":"HAMAP-Rule","id":"MF_01988","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11781092","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9917402","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01988","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10625475","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11781092","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8144675","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9917402","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01988","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	470
Details	Domain: {"description":"ATP-grasp","evidences":[{"source":"HAMAP-Rule","id":"MF_00558","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	16
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00558","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10625475","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00558","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

Catalytic Information from CSA

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

Chain	Residue	Details
A	GLU208
A	HIS246

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

Chain	Residue	Details
D	GLU208
D	HIS246

site_id	CSA3
Number of Residues	2
Details	Annotated By Reference To The Literature 1cqj

Chain	Residue	Details
B	TYR109
B	GLU197

site_id	CSA4
Number of Residues	2
Details	Annotated By Reference To The Literature 1cqj

Chain	Residue	Details
E	TYR109
E	GLU197

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
D	VAL109	electrostatic stabiliser, steric role
D	ASP197	electrostatic stabiliser, modifies pKa

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