Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1CQJ

CRYSTAL STRUCTURE OF 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	6
Details	BINDING SITE FOR RESIDUE PO4 B 904

Chain	Residue
B	GLY52
B	GLY53
B	ARG54
B	GLY55
B	LYS56
B	ASP213

site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PO4 E 905

Chain	Residue
E	LYS56
E	ASP213
E	HOH936
E	HOH973
E	GLY53
E	ARG54
E	GLY55

site_id	AC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE PO4 A 906

Chain	Residue
A	SER153
A	GLY154
A	THR155
A	HIS246
A	HOH962
B	GLY265
B	ALA266
B	GLY267

site_id	AC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PO4 D 907

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

site_id	AC5
Number of Residues	29
Details	BINDING SITE FOR RESIDUE COA A 901

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	SER80
A	ILE95
A	THR96
A	GLU97
A	ASN122
A	CYS123
A	PRO124
A	ILE136
A	HOH911
A	HOH912
A	HOH913
A	HOH927
A	HOH968
E	ARG29
E	GLU33
E	SER36
E	LYS66
E	HOH991

site_id	AC6
Number of Residues	26
Details	BINDING SITE FOR RESIDUE COA D 902

Chain	Residue
B	GLU33
B	SER36
B	LYS66
D	GLY14
D	THR16
D	GLY17
D	SER18
D	GLN19
D	VAL38
D	PRO40
D	LYS42
D	TYR71
D	VAL72
D	PRO73
D	ILE95
D	THR96
D	GLU97
D	ASN122
D	CYS123
D	PRO124
D	ILE136
D	HOH909
D	HOH910
D	HOH923
D	HOH964
D	HOH967

site_id	AC7
Number of Residues	8
Details	BINDING SITE FOR RESIDUE COA B 903

Chain	Residue
B	GLY320
B	GLY321
B	VAL323
B	CYS325
B	GLU350
B	ASN352
B	HOH905
B	HOH1013

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	1
Details	a catalytic site defined by CSA, PubMed 11781092, 17642514, 10625475

Chain	Residue	Details
A	HIS246

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)