Structure of PDB 1w8s Chain B

Receptor sequence
>1w8sB (length=250) Species: 2271 (Thermoproteus tenax) [Search protein sequence]
NLTEKFLRIFARRGKSIILAYDHGIEHGPADFMDNPDSADPEYILRLARD
AGFDGVVFQRGIAEKYYDGSVPLILKLNGKTTLYNGEPVSVANCSVEEAV
SLGASAVGYTIYPGSGFEWKMFEELARIKRDAVKFDLPLVVESFPRGGKV
VNETAPEIVAYAARIALELGADAMKIKYTGDPKTFSWAVKVAGKVPVLMS
GGPKTKTEEDFLKQVEGVLEAGALGIAVGRNVWQRRDALKFARALAELVY
3D structure
PDB1w8s Mechanism of the Schiff base forming fructose-1,6-bisphosphate aldolase: structural analysis of reaction intermediates.
ChainB
Resolution1.85 Å
3D
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
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 FBP B D24 H25 H29 K177 K179 S202 G203 G204 V230 G231 R232 D22 H23 H27 K175 K177 S200 G201 G202 V228 G229 R230
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004332 fructose-bisphosphate aldolase activity
GO:0016829 lyase activity
Biological Process
GO:0006096 glycolytic process
Cellular Component
GO:0005737 cytoplasm

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:1w8s, PDBe:1w8s, PDBj:1w8s
PDBsum1w8s
PubMed15766250
UniProtP58315|ALF1_THETK Fructose-bisphosphate aldolase class 1 (Gene Name=fba)

[Back to BioLiP]