Structure of PDB 1ef9 Chain A

Receptor sequence
>1ef9A (length=261) Species: 562 (Escherichia coli) [Search protein sequence]
MSYQYVNVVTINKVAVIEFNYGRKLNALSKVFIDDLMQALSDLNRPEIRC
IILRAPSGSKVFSAGHDIHELPSGGRDPLSYDDPLRQITRMIQKFPKPII
SMVEGSVWGGAFEMIMSSDLIIAASTSTFSMTPVNLGVPYNLVGIHNLTR
DAGFHIVKELIFTASPITAQRALAVGILNHVVEVEELEDFTLQMAHHISE
KAPLAIAVIKEELRVLGEAHTMNSDEFERIQGMRRAVYDSEDYQEGMNAF
LEKRKPNFVGH
3D structure
PDB1ef9 New reactions in the crotonase superfamily: structure of methylmalonyl CoA decarboxylase from Escherichia coli.
ChainA
Resolution2.7 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) H66 L71 D82 R86 G110 E113 P133 V138 Y140 N141 E228 Y238
Catalytic site (residue number reindexed from 1) H66 L71 D82 R86 G110 E113 P133 V138 Y140 N141 E228 Y238
Enzyme Commision number 4.1.1.-
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 2CP A A64 H66 D67 I68 H69 W108 G110 T132 P133 K253 A64 H66 D67 I68 H69 W108 G110 T132 P133 K253
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004492 methyl/ethyl malonyl-CoA decarboxylase activity
GO:0016829 lyase activity
GO:0016831 carboxy-lyase activity
Biological Process
GO:0006635 fatty acid beta-oxidation
Cellular Component
GO:0005829 cytosol

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:1ef9, PDBe:1ef9, PDBj:1ef9
PDBsum1ef9
PubMed10769118
UniProtP52045|SCPB_ECOLI Methylmalonyl-CoA decarboxylase (Gene Name=scpB)

[Back to BioLiP]