Structure of PDB 1cqi Chain D

Receptor sequence
>1cqiD (length=286) Species: 562 (Escherichia coli) [Search protein sequence]
SILIDKNTKVICQGFTGSQGTFHSEQAIAYGTKMVGGVTPGKGGTTHLGL
PVFNTVREAVAATGATASVIYVPAPFCKDSILEAIDAGIKLIITITEGIP
TLDMLTVKVKLDEAGVRMIGPNCPGVITPGECKIGIQPGHIHKPGKVGIV
SRSGTLTYEAVKQTTDYGFGQSTCVGIGGDPIPGSNFIDILEMFEKDPQT
EAIVMIGEIGGSAEEEAAAYIKEHVTKPVVGYIAGVTAPKGKRMGHAGAI
IAGGKGTADEKFAALEAAGVKTVRSLADIGEALKTV
3D structure
PDB1cqi ADP-binding site of Escherichia coli succinyl-CoA synthetase revealed by x-ray crystallography.
ChainD
Resolution3.3 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 PO4 D S153 G154 T155 H246 S153 G154 T155 H246
BS02 COA D T16 S18 Q19 Y71 V72 P73 T96 C123 I136 T16 S18 Q19 Y71 V72 P73 T96 C123 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)

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:1cqi, PDBe:1cqi, PDBj:1cqi
PDBsum1cqi
PubMed10625475
UniProtP0AGE9|SUCD_ECOLI Succinate--CoA ligase [ADP-forming] subunit alpha (Gene Name=sucD)

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