Structure of PDB 2cjb Chain A

Receptor sequence
>2cjbA (length=474) Species: 269797 (Methanosarcina barkeri str. Fusaro) [Search protein sequence]
SHMKLQFNLKAYFKTKDAIAALFEEANSTLLTRGAPEGQGATEWDRIELT
LQSGRYVRVHDAIFRLRKQLAEIEVESFIIKVPADHELRMLKVPYIKSME
NIEGGIQLELEVGEAEMKNRVPDRILTLLEEKIEAAQEHWNLLWQREPME
HPFKEDPTQAMMKEGWLKRGSSRGQWIHGPQSARIFRTFEKIVLEELLEP
LGYREMIFPKLVTWEVWMKSGHAKGVYPEIYYVCPPQTRDPDYWEEVADY
YKVTHEVPTKLIKEKIAEPIGGMCYAQCPPFWMYVAGETLPNEEIPVKVF
DRSGTSHRYESGGIHGIERVDEFHRIEIVWIGTKEEVLKCAEELHDRYMH
IFNDILDIEWRKARVTPWFMAQEGLLGLAEENTVGTTDYEACLPYRGPDG
EWLEFQNVSINGDKYPKGFNVKLQSGDELWSGCSGVGLERWAAVFLAQKG
LDPANWPEEFRNRVGEMPKGIRFL
3D structure
PDB2cjb Structure of the Unusual Seryl-tRNA Synthetase Reveals a Distinct Zinc-Dependent Mode of Substrate Recognition
ChainA
Resolution2.7 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) C306 R336 E338 R347 E355 D416 E432 N435 C461 R468
Catalytic site (residue number reindexed from 1) C278 R308 E310 R319 E327 D388 E404 N407 C433 R440
Enzyme Commision number 6.1.1.11: serine--tRNA ligase.
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 SER A A304 R353 E355 W396 Q400 A276 R325 E327 W368 Q372
BS02 ZN A C306 E355 C461 C278 E327 C433
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0004812 aminoacyl-tRNA ligase activity
GO:0004828 serine-tRNA ligase activity
GO:0005524 ATP binding
GO:0008270 zinc ion binding
GO:0046872 metal ion binding
Biological Process
GO:0006412 translation
GO:0006434 seryl-tRNA aminoacylation
GO:0016260 selenocysteine biosynthetic process
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:2cjb, PDBe:2cjb, PDBj:2cjb
PDBsum2cjb
PubMed16675947
UniProtQ46AN5|SYS2_METBF Type-2 serine--tRNA ligase (Gene Name=serS2)

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