Structure of PDB 1vbj Chain A

Receptor sequence
>1vbjA (length=281) Species: 5691 (Trypanosoma brucei) [Search protein sequence]
GSPEFMALTQSLKLSNGVMMPVLGFGMWKLQDGNEAETATMWAIKSGYRH
IDTAAIYKNEESAGRAIASCGVPREELFVTTKLWNSDQGYESTLSAFEKS
IKKLGLEYVDLYLIHWPGKDKFIDTWKAFEKLYADKKVRAIGVSNFHEHH
IEELLKHCKVAPMVNQIELHPLLNQKALCEYCKSKNIAVTAWSPLGQGHL
VEDARLKAIGGKYGKTAAQVMLRWEIQAGVITIPKSGNEARIKENGNIFD
FELTAEDIQVIDGMNAGHRYGPDPEVFMNDF
3D structure
PDB1vbj The crystal structure of prostaglandin F synthase from Trypanosoma brucei
ChainA
Resolution2.1 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D47 Y52 K77 H110
Catalytic site (residue number reindexed from 1) D52 Y57 K82 H115
Enzyme Commision number 1.1.1.-
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 NAP A G21 M22 W23 D47 Y52 H110 N140 Q161 W187 S188 P189 L190 Q192 G193 V196 A213 I228 K230 S231 G232 R236 E239 N240 G26 M27 W28 D52 Y57 H115 N145 Q166 W192 S193 P194 L195 Q197 G198 V201 A218 I233 K235 S236 G237 R241 E244 N245
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0004033 aldo-keto reductase (NADPH) activity
GO:0016491 oxidoreductase activity
GO:0016616 oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
GO:0036130 prostaglandin H2 endoperoxidase reductase activity
GO:0045290 D-arabinose 1-dehydrogenase [NAD(P)+] activity
Biological Process
GO:0001516 prostaglandin biosynthetic process
GO:0019571 D-arabinose catabolic process
Cellular Component
GO:0005737 cytoplasm

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Biological Process
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Cellular Component
External links
PDB RCSB:1vbj, PDBe:1vbj, PDBj:1vbj
PDBsum1vbj
PubMed
UniProtQ9GV41|PGFS_TRYBB 9,11-endoperoxide prostaglandin H2 reductase

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