Structure of PDB 7yva Chain A

Receptor sequence
>7yvaA (length=336) Species: 5476 (Candida albicans) [Search protein sequence]
PPAVLSKSGVIYGKDVKDLFDYAQEKGFAIPAINVTSSSTVVAALEAARD
NKAPIILQTSQGGAAYFAGKGVDNKDQAASIAGSIAAAHYIRAIAPTYGI
PVVLHTDHCAKKLLPWFDGMLKADEEFFAKTGTPLFSSHMLDLSEETDDE
NIATCAKYFERMAKMGQWLEMEIGITGGLYTSPETVFAVYESLHKISPNF
SIAAAFGNVHVQLRPEILGDHQVYAKKQIGTDAKHPLYLVFHGGSGSTQE
EFNTAIKNGVVKVNLDTDCQYAYLTGIRDYVTNKIEYLKAPVGNPEGADK
PNKKYFDPRVWVREGEKTMSKRIAEALDIFHTKGQL
3D structure
PDB7yva Crystal structure of Candida albicans Fructose-1,6-bisphosphate aldolase complexed with lipoic acid
ChainA
Resolution2.93 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 4.1.2.13: fructose-bisphosphate aldolase.
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 ZN A H109 E173 H225 H264 H108 E172 H210 H242
Gene Ontology
Molecular Function
GO:0004332 fructose-bisphosphate aldolase activity
GO:0005515 protein binding
GO:0008270 zinc ion binding
GO:0016829 lyase activity
GO:0016832 aldehyde-lyase activity
GO:0046872 metal ion binding
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0006094 gluconeogenesis
GO:0006096 glycolytic process
GO:0051701 biological process involved in interaction with host
GO:0052553 symbiont-mediated perturbation of host immune response
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0005886 plasma membrane
GO:0009277 fungal-type cell wall
GO:0009986 cell surface
GO:0030446 hyphal cell wall

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:7yva, PDBe:7yva, PDBj:7yva
PDBsum7yva
PubMed
UniProtQ9URB4|ALF_CANAL Fructose-bisphosphate aldolase (Gene Name=FBA1)

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