Structure of PDB 1njj Chain C

Receptor sequence
>1njjC (length=352) Species: 31285 (Trypanosoma brucei gambiense) [Search protein sequence]
RFLEGFNTRDALCKKGDPFFVADLGDIVRKHETWKKCLPRVTPFYAVKCN
DDWRVLGTLAALGTGFDCASNTEIQRVRGIGVPPEKIIYANPCKQISHIR
YARDSGVDVMTFDCVDELEKVAKTHPKAKMVLRISTVKFGAKVEDCRFIL
EQAKKLNIDVTGVSFHVGSGSTDASTFAQAISDSRFVFDMGTELGFNMHI
LDIGGGFPGTRDAPLKFEEIAGVINNALEKHFPPDLKLTIVAEPGRYYVA
SAFTLAVNVIAKKVTQSFMYYVNDGVYGSFNCILYDHAVVRPLPQREPIE
KLYPSSVWGPTCDGLDQIVERYYLPEMQVGEWLLFEDMGAYTVVSPTIYY
VV
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.
ChainC
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) K48 H166 E243
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 GET C R22 D243 L339 Q341 L382 E384 R9 D212 L293 Q295 L334 E336 MOAD: Ki=8mM
BS02 ORX C K69 H197 G236 G237 E274 R277 D332 Y389 K48 H166 G205 G206 E243 R246 D286 Y341 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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