Structure of PDB 3err Chain A

Receptor sequence
>3errA (length=527) Species: 10090,300852 [Search protein sequence]
DLKRLRQEPEVFHRAIREKGVALDLEALLAVDEQLHKQQEVIADKQMSVK
EDLDKVEPAVIEAQNAVKSIKKQHLVEVRSMANPPAAVKLALESIALLLG
ESTTDWKQIRSIIMRENFIPTIVNFSAEEISDAIREKMKKNYMSNPSYNY
EIVNRASLAAGPMVKWAIAQLNYADMLKRVEPLRNELQKLEDDAKDNQQK
LEALLLQVPLPPWPGAPVGGEEANREIKRVGGPPEFSFPPLDHVALMEKN
GWWEPRISQVSGSRSYALKGDLALYELALLRFAMDFMARRGFLPMTLPSY
AREKAFLGTGHFPAYRDQVWAIAETDLYLTGTAEVVLNALHSGEILPYEA
LPLRYAGYAPAFRSEAGSFGKDVRGLMRVHQFHKVEQYVLTEASLEASDR
AFQELLENAEEILRLLELPYRLVEVATGDMGPGKWRQVDIEVYLPSEGRY
RETHSCSALLDWQARRANLRYRDPEGRVRYAYTLNNTALATPRILAMLLE
NHQLQDGRVRVPQALIPYMGKEVLEPG
3D structure
PDB3err Structure and functional role of dynein's microtubule-binding domain.
ChainA
Resolution2.27 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R256 R271 E345 S348 R386
Catalytic site (residue number reindexed from 1) R363 R378 E452 S455 R493
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 AMP A R256 E258 M270 V272 F275 E345 T346 S348 T380 R363 E365 M377 V379 F382 E452 T453 S455 T487
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0004812 aminoacyl-tRNA ligase activity
GO:0004828 serine-tRNA ligase activity
GO:0005524 ATP binding
Biological Process
GO:0006418 tRNA aminoacylation for protein translation
GO:0006434 seryl-tRNA aminoacylation

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Molecular Function
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Biological Process
External links
PDB RCSB:3err, PDBe:3err, PDBj:3err
PDBsum3err
PubMed19074350
UniProtQ5SJX7;
Q9JHU4

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