Structure of PDB 2nu8 Chain E

Receptor sequence
>2nu8E (length=385) Species: 562 (Escherichia coli) [Search protein sequence]
MNLHEYQAKQLFARYGLPAPVGYACTTPREAEEAASKIGAGPWVVKCQVH
AGGRGKAGGVKVVNSKEDIRAFAENWLGKRLVTYQTDANGQPVNQILVEA
ATDIAKELYLGAVVDRSSRRVVFMASTEGGVEIEKVAEETPHLIHKVALD
PLTGPMPYQGRELAFKLGLEGKLVQQFTKIFMGLATIFLERDLALIEINP
LVITKQGDLICLDGKLGADGNALFRQPDLREMRDQSQEDPREAQAAQWEL
NYVALDGNIGCMVNGAGLAMGTMDIVKLHGGEPANFLDVGGGATKERVTE
AFKIILSDDKVKAVLVNIFGGIVRCDLIADGIIGAVAEVGVNVPVVVRLE
GNNAELGAKKLADSGLNIIAAKGLTDAAQQVVAAV
3D structure
PDB2nu8 Participation of Cys 123alpha of Escherichia coli Succinyl-CoA Synthetase in Catalysis
ChainE
Resolution2.15 Å
3D
structure
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Enzymatic activity
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 E E33 S36 K66 E33 S36 K66
BS02 COA E G320 G321 V323 C325 I328 E350 N352 G320 G321 V323 C325 I328 E350 N352
Gene Ontology
Molecular Function
GO:0000287 magnesium ion 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:0005524 ATP binding
GO:0016874 ligase activity
GO:0046872 metal ion binding
Biological Process
GO:0006099 tricarboxylic acid cycle
GO:0006104 succinyl-CoA metabolic process
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0009361 succinate-CoA ligase complex (ADP-forming)
GO:0042709 succinate-CoA ligase complex

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2nu8, PDBe:2nu8, PDBj:2nu8
PDBsum2nu8
PubMed17642514
UniProtP0A836|SUCC_ECOLI Succinate--CoA ligase [ADP-forming] subunit beta (Gene Name=sucC)

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