Structure of PDB 1aw1 Chain G

Receptor sequence
>1aw1G (length=255) Species: 90736 (Moritella marina) [Search protein sequence]
RHPVVMGNWKLNGSKEMVVDLLNGLNAELEGVTGVDVAVAPPALFVDLAE
RTLTEAGSAIILGAQNTDLNNSGAFTGDMSPAMLKEFGATHIIIGHSERR
EYHAESDEFVAKKFAFLKENGLTPVLCIGESDAQNEAGETMAVCARQLDA
VINTQGVEALEGAIIAYEPIWAIGTGKAATAEDAQRIHAQIRAHIAEKSE
AVAKNVVIQYGGSVKPENAAAYFAQPDIDGALVGGAALDAKSFAAIAKAA
AEAKA
3D structure
PDB1aw1 Triose-phosphate isomerase (TIM) of the psychrophilic bacterium Vibrio marinus. Kinetic and structural properties.
ChainG
Resolution2.7 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) N9 K11 H97 E99 E169 G175 S214
Catalytic site (residue number reindexed from 1) N8 K10 H96 E98 E168 G174 S213
Enzyme Commision number 5.3.1.1: triose-phosphate 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 PGA G K11 H97 E169 L233 G235 G236 K10 H96 E168 L232 G234 G235
Gene Ontology
Molecular Function
GO:0004807 triose-phosphate isomerase activity
GO:0016853 isomerase activity
Biological Process
GO:0006094 gluconeogenesis
GO:0006096 glycolytic process
GO:0019563 glycerol catabolic process
GO:0046166 glyceraldehyde-3-phosphate biosynthetic process
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1aw1, PDBe:1aw1, PDBj:1aw1
PDBsum1aw1
PubMed9442062
UniProtP50921|TPIS_MORMI Triosephosphate isomerase (Gene Name=tpiA)

[Back to BioLiP]