Structure of PDB 1szr Chain D

Receptor sequence
>1szrD (length=368) Species: 5702 (Trypanosoma brucei brucei) [Search protein sequence]
RFLEGFNTRDALCKKISGDPFFVADLGDIVRKHETWKKCLPRVTPFYAVK
CNDDWRVLGTLAALGTGFDCASNTEIQRVRGIGVPPEKIIYANPCKQISH
IRYARDSGVDVMTFDCVDELEKVAKTHPKAKMVLRISTVKFGAKVEDCRF
ILEQAKKLNIDVTGVSFHVGSGSTDASTFAQAISDSRFVFDMGTELGFNM
HILDIGGGFPGTRDAPLKFEEIAGVINNALEKHFPPDLKLTIVAEPGRYY
VASAFTLAVNVIAKAVTPAQSFMYYVNDGVYGSFNCILYDHAVVRPLPQR
EPIPNEKLYPSSVWGPTCDGLDQIVERYYLPEMQVGEWLLFEDMGAYTVV
GTSSFNGFQSPTIYYVVS
3D structure
PDB1szr Multiple active site conformations revealed by distant site mutation in ornithine decarboxylase
ChainD
Resolution2.15 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) K69 H197 E274
Catalytic site (residue number reindexed from 1) K50 H168 E245
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 PXP D K69 R154 H197 G237 E274 G276 R277 Y389 K50 R135 H168 G208 E245 G247 R248 Y347
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004586 ornithine decarboxylase activity
GO:0016831 carboxy-lyase activity
Biological Process
GO:0006596 polyamine biosynthetic process
GO:0033387 putrescine biosynthetic process from ornithine
Cellular Component
GO:0005737 cytoplasm

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1szr, PDBe:1szr, PDBj:1szr
PDBsum1szr
PubMed15476392
UniProtP07805|DCOR_TRYBB Ornithine decarboxylase

[Back to BioLiP]