Structure of PDB 2nu6 Chain A

Receptor sequence
>2nu6A (length=287) Species: 562 (Escherichia coli) [Search protein sequence]
SILIDKNTKVICQGFTGSQGTFHSEQAIAYGTKMVGGVTPGKGGTTHLGL
PVFNTVREAVAATGATASVIYVPAPFCKDSILEAIDAGIKLIITITEGIP
TLDMLTVKVKLDEAGVRMIGPNAPGVITPGECKIGIQPGHIHKPGKVGIV
SRSGTLTYEAVKQTTDYGFGQSTCVGIGGDPIPGSNFIDILEMFEKDPQT
EAIVMIGEIGGSAEEEAAAYIKEHVTKPVVGYIAGVTAPKGKRMGHAGAI
IAGGKGTADEKFAALEAAGVKTVRSLADIGEALKTVL
3D structure
PDB2nu6 Participation of Cys 123alpha of Escherichia coli Succinyl-CoA Synthetase in Catalysis
ChainA
Resolution2.55 Å
3D
structure
Catalytic site residues are labeled in the structure
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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 G14 T16 G17 S18 Q19 P40 K42 Y71 V72 P73 S80 T96 E97 N122 A123 P124 G14 T16 G17 S18 Q19 P40 K42 Y71 V72 P73 S80 T96 E97 N122 A123 P124
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)

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:2nu6, PDBe:2nu6, PDBj:2nu6
PDBsum2nu6
PubMed17642514
UniProtP0AGE9|SUCD_ECOLI Succinate--CoA ligase [ADP-forming] subunit alpha (Gene Name=sucD)

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