Structure of PDB 6tnm Chain A

Receptor sequence
>6tnmA (length=719) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
MLYKGDTLYLDWLEDGIAELVFDAPGSVNKLDTATVASLGEAIGVLEQQS
DLKGLLLRSNKAAFIVGADITEFLSLFLVPEEQLSQWLHFANSVFNRLED
LPVPTIAAVNGYALGGGCECVLATDYRLATPDLRIGLPETKLGIMPGFGG
SVRMPRMLGADSALEIIAAGKDVGADQALKIGLVDGVVKAEKLVEGAKAV
LRQAINGDLDWKAKRQPKLEPLKLSKIEATMSFTIAKGMVAQTAGKHYPA
PITAVKTIEAAARFGREEALNLENKSFVPLAHTNEARALVGIFLNDQYVK
GKAKKLTKDVETPKQAAVLGAGIMGGGIAYQSAWKGVPVVMKDINDKSLT
LGMTEAAKLLNKQLERGKIDGLKLAGVISTIHPTLDYAGFDRVDIVVEAV
VENPKVKKAVLAETEQKVRQDTVLASNTSTIPISELANALERPENFCGMH
FFNPVHRMPLVEIIRGEKSSDETIAKVVAWASKMGKTPIVVNDCPGFFVN
RVLFPYFAGFSQLLRDGADFRKIDKVMEKQFGWPMGPAYLLDVVGIDTAH
HAQAVMAAGFPQRMQKDYRDAIDALFDANRFGQKNGLGFWRYKEDSKGKP
KKEEDAAVEDLLAEVSQPKRDFSEEEIIARMMIPMVNEVVRCLEEGIIAT
PAEADMALVYGLGFPPFHGGAFRWLDTLGSAKYLDMAQQYQHLGPLYEVP
EGLRNKARHNEPYYPPVEP
3D structure
PDB6tnm Insights into the stability and substrate specificity of the E. coli aerobic beta-oxidation trifunctional enzyme complex.
ChainA
Resolution2.95 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) A68 F73 G116 E119 P138 E139 G147 N271 S429 H450 E462 N500
Catalytic site (residue number reindexed from 1) A68 F73 G116 E119 P138 E139 G147 N271 S429 H450 E462 N500
Enzyme Commision number 1.1.1.35: 3-hydroxyacyl-CoA dehydrogenase.
4.2.1.17: enoyl-CoA hydratase.
5.1.2.3: 3-hydroxybutyryl-CoA epimerase.
5.3.3.8: Delta(3)-Delta(2)-enoyl-CoA isomerase.
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 ATP A D343 I344 V400 V401 V406 K584 D343 I344 V400 V401 V406 K584
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0003857 3-hydroxyacyl-CoA dehydrogenase activity
GO:0004165 delta(3)-delta(2)-enoyl-CoA isomerase activity
GO:0004300 enoyl-CoA hydratase activity
GO:0008692 3-hydroxybutyryl-CoA epimerase activity
GO:0016491 oxidoreductase activity
GO:0016509 long-chain-3-hydroxyacyl-CoA dehydrogenase activity
GO:0016616 oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
GO:0016829 lyase activity
GO:0016853 isomerase activity
GO:0070403 NAD+ binding
Biological Process
GO:0006631 fatty acid metabolic process
GO:0006635 fatty acid beta-oxidation
GO:0009056 catabolic process
GO:0009062 fatty acid catabolic process
GO:0016042 lipid catabolic process
Cellular Component
GO:0036125 fatty acid beta-oxidation multienzyme complex

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:6tnm, PDBe:6tnm, PDBj:6tnm
PDBsum6tnm
PubMed32171906
UniProtP21177|FADB_ECOLI Fatty acid oxidation complex subunit alpha (Gene Name=fadB)

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