Structure of PDB 1jkj Chain D

Receptor sequence

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

SILIDKNTKVICQGFTGSQGTFHSEQAIAYGTKMVGGVTPGKGGTTHLGL
PVFNTVREAVAATGATASVIYVPAPFCKDSILEAIDAGIKLIITITEGIP
TLDMLTVKVKLDEAGVRMIGPNCPGVITPGECKIGIQPGHIHKPGKVGIV
SRSGTLTYEAVKQTTDYGFGQSTCVGIGGDPIPGSNFIDILEMFEKDPQT
EAIVMIGEIGGSAEEEAAAYIKEHVTKPVVGYIAGVTAPKGKRMGHAGAI
IAGGKGTADEKFAALEAAGVKTVRSLADIGEALKTVL

3D structure

• PDB: 1jkj 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: 2.35 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 G17 S18 Q19 V38 P40 K42 Y71 V72 P73 S80 T96 E97 C123 P124 I136	G14 T16 G17 S18 Q19 V38 P40 K42 Y71 V72 P73 S80 T96 E97 C123 P124 I136

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