Structure of PDB 6ybp Chain F

Receptor sequence
>6ybpF (length=506) Species: 272630 (Methylorubrum extorquens AM1) [Search protein sequence]
LEKLEERRAQARLGGGEKRLEAQHKRGKLTARERIELLLDHGSFEEFDMF
VQHRSTDFGMEKQKIPGDGVVTGWGTVNGRTVFLFSKDFTVFGGSLSEAH
AAKIVKVQDMALKMRAPIIGIFDAGGARIQEGVAALGGYGEVFRRNVAAS
GVIPQISVIMGPCAGGDVYSPAMTDFIFMVRDTSYMFVTGPDVVKTVTNE
VVTAEELGGAKVHTSKSSIADGSFENDVEAILQIRRLLDFLPANNIEGVP
EIESFDDVNRLDKSLDTLIPDNPNKPYDMGELIRRVVDEGDFFEIQAAYA
RNIITGFGRVEGRTVGFVANQPLVLAGVLDSDASRKAARFVRFCNAFSIP
IVTFVDVPGFLPGTAQEYGGLIKHGAKLLFAYSQATVPLVTIITRKAFGG
AYDVMASKHVGADLNYAWPTAQIAVMGAKGAVEIIFRAEIGDADKIAERT
KEYEDRFLSPFVAAERGYIDEVIMPHSTRKRIARALGMLRTKEMEQPWKK
HDNIPL
3D structure
PDB6ybp A new-to-nature carboxylation module to improve natural and synthetic CO2 fixation
ChainF
Resolution3.48 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) G169 G170 G404 A405
Catalytic site (residue number reindexed from 1) G165 G166 G400 A401
Enzyme Commision number 6.4.1.3: propionyl-CoA carboxylase.
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 F R23 G129 R19 G125
BS02 BTI F F364 P366 F360 P362
Gene Ontology
Molecular Function
GO:0004658 propionyl-CoA carboxylase activity
GO:0016874 ligase activity

View graph for
Molecular Function
External links
PDB RCSB:6ybp, PDBe:6ybp, PDBj:6ybp
PDBsum6ybp
PubMed
UniProtC5AP75

[Back to BioLiP]