Structure of PDB 4b3i Chain A

Receptor sequence
>4b3iA (length=731) Species: 83332 (Mycobacterium tuberculosis H37Rv) [Search protein sequence]
MGSSHHHHHHSMPDNTIQWDKDADGIVTLTMDDPSGSTNVMNEAYIESMG
KAVDRLVAEKDSITGVVVASAKKTFFAGGDVKTMIQARPEDAGDVFNTVE
TIKRQLRTLETLGKPVVAAINGAALGGGLEIALACHHRIAADVKGSQLGL
PEVTLGLLPGGGGVTRTVRMFGIQNAFVSVLAQGTRFKPAKAKEIGLVDE
LVATVEELVPAAKAWIKEELKANPDGAGVQPWDKKGYKMPGGTPSSPGLA
AILPSFPSNLRKQLKGAPMPAPRAILAAAVEGAQVDFDTASRIESRYFAS
LVTGQVAKNMMQAFFFDLQAINAGGSRPEGIGKTPIKRIGVLGAGMMGAG
IAYVSAKAGYEVVLKDVSLEAAAKGKGYSEKLEAKALERGRTTQERSDAL
LARITPTADAADFKGVDFVIEAVFENQELKHKVFGEIEDIVEPNAILGSN
TSTLPITGLATGVKRQEDFIGIHFFSPVDKMPLVEIIKGEKTSDEALARV
FDYTLAIGKTPIVVNDSRGFFTSRVIGTFVNEALAMLGEGVEPASIEQAG
SQAGYPAPPLQLSDELNLELMHKIAVATRKGVEDAGGTYQPHPAEAVVEK
MIELGRSGRLKGAGFYEYADGKRSGLWPGLRETFKSGSSQPPLQDMIDRM
LFAEALETQKCLDEGVLTSTADANIGSIMGIGFPPWTGGSAQFIVGYSGP
AGTGKAAFVARARELAAAYGDRFLPPESLLS
3D structure
PDB4b3i Structure of Mycobacterial Beta-Oxidation Trifunctional Enzyme Reveals its Altered Assembly and Putative Substrate Channeling Pathway.
ChainA
Resolution2.63 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) G68 E89 R93 G116 E119 P140 E141 G149 S441 H462 E474 S512
Catalytic site (residue number reindexed from 1) G79 E100 R104 G127 E130 P151 E152 G160 S452 H473 E485 S523
Enzyme Commision number 1.1.1.35: 3-hydroxyacyl-CoA dehydrogenase.
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 A T27 V29 A66 G68 D69 V70 E141 F304 Q308 T38 V40 A77 G79 D80 V81 E152 F315 Q319
BS02 ADP A Q629 P630 P631 L632 Q633 Q640 P641 P642 L643 Q644
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0003857 3-hydroxyacyl-CoA dehydrogenase activity
GO:0004300 enoyl-CoA hydratase 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:0070403 NAD+ binding
Biological Process
GO:0006631 fatty acid metabolic process
GO:0006635 fatty acid beta-oxidation
GO:0009056 catabolic process
GO:0016042 lipid catabolic process
Cellular Component
GO:0005829 cytosol
GO:0005886 plasma membrane
GO:0009274 peptidoglycan-based cell wall

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4b3i, PDBe:4b3i, PDBj:4b3i
PDBsum4b3i
PubMed23496842
UniProtO53872

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