Structure of PDB 6n93 Chain A

Receptor sequence
>6n93A (length=260) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
AYQYVNVVTINKVAVIEFNYGRKLNALSKVFIDDLMQALSDLNRPEIRCI
ILRAPSGSKVFSAGHDIHELPSGGRDPLSYDDPLRQITRMIQKFPKPIIS
MVEGSVWGGAFEMIMSSDLIIAASTSTFSMTPVNLGVPYNLVGIHNLTRD
AGFHIVKELIFTASPITAQRALAVGILNHVVEVEELEDFTLQMAHHISEK
APLAIAVIKEELRVLGEAHTMNSDEFERIQGMRRAVYDSEDYQEGMNAFL
EKRKPNFVGH
3D structure
PDB6n93 Sulfonate/Nitro Bearing Methylmalonyl-Thioester Isosteres Applied to Methylmalonyl-CoA Decarboxylase Structure-Function Studies.
ChainA
Resolution1.7 Å
3D
structure
Catalytic site residues are labeled in the structure
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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 KGA A L25 A64 H66 D67 I68 H69 W108 T132 L136 F250 K253 L24 A63 H65 D66 I67 H68 W107 T131 L135 F249 K252 MOAD: Ki=20.6uM
PDBbind-CN: -logKd/Ki=4.69,Kd=20.6uM
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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:6n93, PDBe:6n93, PDBj:6n93
PDBsum6n93
PubMed30869886
UniProtP52045|SCPB_ECOLI Methylmalonyl-CoA decarboxylase (Gene Name=scpB)

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