Structure of PDB 1jll Chain D

Receptor sequence

>1jllD (length=287) Species: 562 (Escherichia coli)

SILIDKNTKVICQGFTGSQGTFHSEQAIAYGTKMVGGVTPGKGGTTHLGL
PVFNTVREAVAATGATASVIYVPAPFCKDSILEAIDAGIKLIITITEGIP
TLDMLTVKVKLDEAGVRMIGPNCPGVITPGECKIGIQPGHIHKPGKVGIV
SRSGTLTYEAVKQTTDYGFGQSTCVGIGGDPIPGSNFIDILEMFEKDPQT
EAIVMIGEIGGSAEEEAAAYIKEHVTKPVVGYIAGVTAPKGKRMGHAGAI
IAGGKGTADEKFAALEAAGVKTVRSLADIGEALKTVL

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: D
• Resolution: 2.69 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): E208 H246
• Catalytic site (residue number reindexed from 1): E208 H246
• 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	D	G14 T16 S18 Q19 P40 K42 Y71 V72 P73 S80 T96 E97 C123	G14 T16 S18 Q19 P40 K42 Y71 V72 P73 S80 T96 E97 C123

Gene Ontology

Molecular Function

• GO:0000166 nucleotide 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:0016874 ligase activity

Biological Process

• GO:0006099 tricarboxylic acid cycle

Cellular Component

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

External links

• PDB: RCSB:1jll, PDBe:1jll, PDBj:1jll
• PDBsum: 1jll
• PubMed: 11781092
• UniProt: P0AGE9|SUCD_ECOLI Succinate--CoA ligase [ADP-forming] subunit alpha (Gene Name=sucD)