Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1JLL

Crystal Structure Analysis of the E197betaA Mutant of E. coli SCS

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
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
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	7
Details	BINDING SITE FOR RESIDUE PO4 A 1600

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

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 B 1400

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

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 B 1500

Chain	Residue
A	ARG243
B	MET1
B	GLY220
B	ARG233

site_id	AC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PO4 D 1601

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

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 E 1401

Chain	Residue
E	GLY52
E	GLY53
E	ARG54
E	GLY55
E	ASP213

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 E 1501

Chain	Residue
D	ARG243
E	MET1
E	GLY220
E	ARG233

site_id	AC7
Number of Residues	25
Details	BINDING SITE FOR RESIDUE COA A 1300

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	THR96
A	GLU97
A	CYS123
A	HOH1605
A	HOH1610
A	HOH1635
A	HOH1643
A	HOH1647
B	ARG161
E	ARG29
E	GLU33
E	SER36
E	LYS66

site_id	AC8
Number of Residues	24
Details	BINDING SITE FOR RESIDUE COA D 1301

Chain	Residue
B	ARG29
B	GLU33
B	SER36
B	LYS66
B	HOH1926
B	HOH1932
D	GLY14
D	THR16
D	GLY17
D	SER18
D	GLN19
D	VAL38
D	PRO40
D	LYS42
D	TYR71
D	VAL72
D	PRO73
D	SER80
D	THR96
D	GLU97
D	CYS123
D	HOH1630
D	HOH1631
E	ARG161

site_id	AC9
Number of Residues	8
Details	BINDING SITE FOR RESIDUE COA B 1903

Chain	Residue
B	ILE318
B	GLY320
B	GLY321
B	ILE322
B	VAL323
B	CYS325
B	GLU350
B	ASN352

site_id	BC1
Number of Residues	9
Details	BINDING SITE FOR RESIDUE COA E 1904

Chain	Residue
E	ILE318
E	GLY320
E	GLY321
E	ILE322
E	VAL323
E	CYS325
E	GLU350
E	GLY351
E	ASN352

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	ALA197

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

Chain	Residue	Details
E	TYR109
E	ALA197

site_id	MCSA1
Number of Residues	2
Details	M-CSA 476

Chain	Residue	Details
B	TYR109	electrostatic stabiliser, steric role
B	ALA197	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)