Structure of PDB 1jll Chain E

Receptor sequence

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

MNLHEYQAKQLFARYGLPAPVGYACTTPREAEEAASKIGAGPWVVKCQVH
AGGRGKAGGVKVVNSKEDIRAFAENWLGKRLVTYQTDANGQPVNQILVEA
ATDIAKELYLGAVVDRSSRRVVFMASTEGGVEIEKVAEETPHLIHKVALD
PLTGPMPYQGRELAFKLGLEGKLVQQFTKIFMGLATIFLERDLALIAINP
LVITKQGDLICLDGKLGADGNALFRQPDLREMRDQSQEDPREAQAAQWEL
NYVALDGNIGCMVNGAGLAMGTMDIVKLHGGEPANFLDVGGGATKERVTE
AFKIILSDDKVKAVLVNIFGGIVRCDLIADGIIGAVAEVGVNVPVVVRLE
GNNAELGAKKLADSGLNIIAAKGLTDAAQQVVAAV

3D structure

• PDB: 1jll Two glutamate residues, Glu 208 alpha and Glu 197 beta, are crucial for phosphorylation and dephosphorylation of the active-site histidine residue in succinyl-CoA synthetase.
• Chain: E
• Resolution: 2.69 Å

Enzymatic activity

• 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	COA	E	E33 S36 K66	E33 S36 K66
BS02	COA	E	G320 G321 I322 V323 C325 E350	G320 G321 I322 V323 C325 E350

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:1jll, PDBe:1jll, PDBj:1jll
• PDBsum: 1jll
• PubMed: 11781092
• UniProt: P0A836|SUCC_ECOLI Succinate--CoA ligase [ADP-forming] subunit beta (Gene Name=sucC)