Structure of PDB 1njj Chain D

Receptor sequence
>1njjD (length=354) Species: 31285 (Trypanosoma brucei gambiense) [Search protein sequence]
NTRDALCKKISGDPFFVADLGDIVRKHETWKKCLPRVTPFYAVKCNDDWR
VLGTLAALGTGFDCASNTEIQRVRGIGVPPEKIIYANPCKQISHIRYARD
SGVDVMTFDCVDELEKVAKTHPKAKMVLRISTVKFGAKVEDCRFILEQAK
KLNIDVTGVSFHVGSGSTDASTFAQAISDSRFVFDMGTELGFNMHILDIG
GGFPGTRDAPLKFEEIAGVINNALEKHFPPDLKLTIVAEPGRYYVASAFT
LAVNVIAKKVTSNAQSFMYYVNDGVYGSFNCILYDHAVVRPLPQREPIPN
EKLYPSSVWGPTCDGLDQIVERYYLPEMQVGEWLLFEDMGAYTVFQSPTI
YYVV
3D structure
PDB1njj X-ray Structure Determination of Trypanosoma brucei Ornithine Decarboxylase Bound to D-Ornithine and to G418: INSIGHTS INTO SUBSTRATE BINDING AND ODC CONFORMATIONAL FLEXIBILITY.
ChainD
Resolution2.45 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K69 H197 E274
Catalytic site (residue number reindexed from 1) K44 H162 E239
Enzyme Commision number 4.1.1.17: ornithine decarboxylase.
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 ORX D C360 D361 C313 D314 MOAD: Kd=0.27mM
BS02 ORX D K69 H197 G237 E274 G276 R277 Y331 D332 Y389 K44 H162 G202 E239 G241 R242 Y284 D285 Y342 MOAD: Kd=0.27mM
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004586 ornithine decarboxylase activity
GO:0016829 lyase activity
Biological Process
GO:0006596 polyamine biosynthetic process
GO:0033387 putrescine biosynthetic process from ornithine
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1njj, PDBe:1njj, PDBj:1njj
PDBsum1njj
PubMed12672797
UniProtQ9TZZ6

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