Structure of PDB 1ci7 Chain A

Receptor sequence
>1ci7A (length=292) Species: 4754 (Pneumocystis carinii) [Search protein sequence]
NAEEQQYLNLVQYIINHGEDRPDRTGTGTLSVFAPSPLKFSLRNKTFPLL
TTKRVFIRGVIEELLWFIRGETDSLKLREKNIHIWDANGSREYLDSIGLT
KRQEGDLGPIYGFQWRHFGAEYIDCKTNYIGQGVDQLANIIQKIRTSPYD
RRLILSAWNPADLEKMALPPCHMFCQFYVHIPSRPELSCQLYQRSCDMGL
GVPFNIASYALLTCMIAHVCDLDPGDFIHVMGDCHIYKDHIEALQQQLTR
SPRPFPTLSLNRSITDIEDFTLDDFNIQNYHPYETIKMKMSI
3D structure
PDB1ci7 The structural mechanism for half-the-sites reactivity in an enzyme, thymidylate synthase, involves a relay of changes between subunits.
ChainA
Resolution2.6 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) E65 W87 Y113 C173 R199 D202
Catalytic site (residue number reindexed from 1) E63 W85 Y111 C171 R194 D197
Enzyme Commision number 2.1.1.45: thymidylate synthase.
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 UMP A C173 R199 S200 D202 N210 C171 R194 S195 D197 N205
BS02 UMP A R153 R154 R151 R152
Gene Ontology
Molecular Function
GO:0004799 thymidylate synthase activity
GO:0008168 methyltransferase activity
GO:0016741 transferase activity, transferring one-carbon groups
Biological Process
GO:0006231 dTMP biosynthetic process
GO:0006235 dTTP biosynthetic process
GO:0009165 nucleotide biosynthetic process
GO:0032259 methylation
Cellular Component
GO:0005739 mitochondrion
GO:0005829 cytosol

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Cellular Component
External links
PDB RCSB:1ci7, PDBe:1ci7, PDBj:1ci7
PDBsum1ci7
PubMed10529228
UniProtP13100|TYSY_PNECA Thymidylate synthase (Gene Name=THYA)

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