Structure of PDB 6k7s Chain A

Receptor sequence
>6k7sA (length=278) Species: 6689 (Penaeus vannamei) [Search protein sequence]
MRHDEYQYLDLIRQIMRTGNRKGDRTGTGTISMFGAQMRYSLRDGIFPLL
TTKRVFWRGVAEELLWFVRGSTNAKELQEKDIHIWDGNSSREEGDLGPVY
GFQWRHFGAPYADMHTDYTGQGVDQLQQVIDTIKNNPDDRRIIMCAWNPV
DVPKMALPPCHCLCQFYVANGELSCQLYQRSADMGLGVPFNIASYALLTY
MIAHVTDLKPGDFVHTLGDAHVYSNHCEALEEQLKREPRPFPSLKIKRKV
ENISDFKFEDFELDGYKPHPKIKMEMAV
3D structure
PDB6k7s Structural analysis of a shrimp thymidylate synthase reveals species-specific interactions with dUMP and raltitrexed.
ChainA
Resolution1.56 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) E63 W85 Y111 C171 R191 D194
Catalytic site (residue number reindexed from 1) E63 W85 Y100 C160 R180 D183
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 R25 C171 R191 S192 D194 N202 H232 Y234 R25 C160 R180 S181 D183 N191 H221 Y223
BS02 D16 A F56 I84 D194 L197 G198 F201 Y234 M287 A288 F56 I84 D183 L186 G187 F190 Y223 M276 A277
BS03 UMP A R151 R152 R140 R141
Gene Ontology
Molecular Function
GO:0004799 thymidylate synthase activity
GO:0016741 transferase activity, transferring one-carbon groups
Biological Process
GO:0006231 dTMP biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:6k7s, PDBe:6k7s, PDBj:6k7s
PDBsum6k7s
PubMed
UniProtA0A423U5Z1

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