Structure of PDB 2scu Chain A

Receptor sequence
>2scuA (length=286) Species: 562 (Escherichia coli) [Search protein sequence]
SILIDKNTKVICQGFTGSQGTFHSEQAIAYGTKMVGGVTPGKGGTTHLGL
PVFNTVREAVAATGATASVIYVPAPFCKDSILEAIDAGIKLIITITEGIP
TLDMLTVKVKLDEAGVRMIGPNCPGVITPGECKIGIQPGHIHKPGKVGIV
SRSGTLTYEAVKQTTDYGFGQSTCVGIGGDPIPGSNFIDILEMFEKDPQT
EAIVMIGEIGGSAEEEAAAYIKEHVTKPVVGYIAGVTAPKGKRMGHAGAI
IAGGKGTADEKFAALEAAGVKTVRSLADIGEALKTV
3D structure
PDB2scu A detailed structural description of Escherichia coli succinyl-CoA synthetase.
ChainA
Resolution2.3 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 A T16 G17 S18 Q19 P40 K42 V72 P73 I95 T96 N122 C123 P124 I136 T16 G17 S18 Q19 P40 K42 V72 P73 I95 T96 N122 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)

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:2scu, PDBe:2scu, PDBj:2scu
PDBsum2scu
PubMed9917402
UniProtP0AGE9|SUCD_ECOLI Succinate--CoA ligase [ADP-forming] subunit alpha (Gene Name=sucD)

[Back to BioLiP]