Structure of PDB 1cqi Chain E

Receptor sequence

>1cqiE (length=385) Species: 562 (Escherichia coli)

MNLHEYQAKQLFARYGLPAPVGYACTTPREAEEAASKIGAGPWVVKCQVH
AGGRGKAGGVKVVNSKEDIRAFAENWLGKRLVTYQTDANGQPVNQILVEA
ATDIAKELYLGAVVDRSSRRVVFMASTEGGVEIEKVAEETPHLIHKVALD
PLTGPMPYQGRELAFKLGLEGKLVQQFTKIFMGLATIFLERDLALIEINP
LVITKQGDLICLDGKLGADGNALFRQPDLREMRDQSQEDPREAQAAQWEL
NYVALDGNIGCMVNGAGLAMGTMDIVKLHGGEPANFLDVGGGATKERVTE
AFKIILSDDKVKAVLVNIFGGIVRCDLIADGIIGAVAEVGVNVPVVVRLE
GNNAELGAKKLADSGLNIIAAKGLTDAAQQVVAAV

3D structure

• PDB: 1cqi ADP-binding site of Escherichia coli succinyl-CoA synthetase revealed by x-ray crystallography.
• Chain: E
• Resolution: 3.3 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): Y109 E197
• Catalytic site (residue number reindexed from 1): Y109 E197
• Enzyme Commision number: 6.2.1.5: succinate--CoA ligase (ADP-forming).

Interaction with ligand

Site #	Ligand	Ligand chain	Binding residues on receptor (original residue number in PDB)	Binding residues on receptor (residue number reindexed from 1)	Binding affinity
BS01	MG	E	N199 D213	N199 D213
BS02	ADP	E	V44 K46 R54 G55 A101 T102 L212 D213	V44 K46 R54 G55 A101 T102 L212 D213

Gene Ontology

Molecular Function

• GO:0000287 magnesium ion binding
• GO:0003824 catalytic activity
• GO:0004775 succinate-CoA ligase (ADP-forming) activity
• GO:0004776 succinate-CoA ligase (GDP-forming) activity
• GO:0005515 protein binding
• GO:0005524 ATP binding
• GO:0016874 ligase activity
• GO:0046872 metal ion binding

Biological Process

• GO:0006099 tricarboxylic acid cycle
• GO:0006104 succinyl-CoA metabolic process

Cellular Component

• GO:0005737 cytoplasm
• GO:0005829 cytosol
• GO:0009361 succinate-CoA ligase complex (ADP-forming)
• GO:0042709 succinate-CoA ligase complex

External links

• PDB: RCSB:1cqi, PDBe:1cqi, PDBj:1cqi
• PDBsum: 1cqi
• PubMed: 10625475
• UniProt: P0A836|SUCC_ECOLI Succinate--CoA ligase [ADP-forming] subunit beta (Gene Name=sucC)