Structure of PDB 6n92 Chain E

Receptor sequence
>6n92E (length=260) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
AYQYVNVVTINKVAVIEFNYGRKLNALSKVFIDDLMQALSDLNRPEIRCI
ILRAPSGSKVFSAGHDIHELPSGGRDPLSYDDPLRQITRMIQKFPKPIIS
MVEGSVWGGAFEMIMSSDLIIAASTSTFSMTPVNLGVPYNLVGIHNLTRD
AGFHIVKELIFTASPITAQRALAVGILNHVVEVEELEDFTLQMAHHISEK
APLAIAVIKEELRVLGEAHTMNSDEFERIQGMRRAVYDSEDYQEGMNAFL
EKRKPNFVGH
3D structure
PDB6n92 Sulfonate/Nitro Bearing Methylmalonyl-Thioester Isosteres Applied to Methylmalonyl-CoA Decarboxylase Structure-Function Studies.
ChainE
Resolution1.7 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 G110 E113 P133 V138 Y140 E228 Y238
Catalytic site (residue number reindexed from 1) H65 L70 G109 E112 P132 V137 Y139 E227 Y237
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 KFV E K24 L25 A64 H66 D67 I68 G109 G110 T132 P133 F250 K23 L24 A63 H65 D66 I67 G108 G109 T131 P132 F249 MOAD: Ki=10.8uM
BS02 KFV E S106 V107 W108 T128 F129 S130 S165 P166 S105 V106 W107 T127 F128 S129 S164 P165 MOAD: Ki=10.8uM
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:6n92, PDBe:6n92, PDBj:6n92
PDBsum6n92
PubMed30869886
UniProtP52045|SCPB_ECOLI Methylmalonyl-CoA decarboxylase (Gene Name=scpB)

[Back to BioLiP]