Structure of PDB 1um2 Chain B Binding Site BS01
Receptor Information
>1um2 Chain B (length=419) Species:
4932
(Saccharomyces cerevisiae) [
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SFAKGTNVLMADGSIECIENIEVGNKVMGKDGRPREVIKLPRGRETMYSV
VQKELLKFTCNATNELVVRTPRSVRRLSRTIKGVEYFEVITFEMGQKKAP
DGRIVELVKEVSKSYPISEGPERANELVESYRKASNKAYFEWTIEARDLS
LLGSHVRKATYQTYAPILYENDHFFDYMQKSKFHLTIEGPKVLAYLLGLW
IGDGLSDRATFSVDSRDTSLMERVTEYAEKLNLCAEYKDRKEPQVAKTVN
LYSLNTENPLWDAIVGLGFLKDGVKNIPSFLSTDNIGTRETFLAGLIDSD
GYVTDEHGIKATIKTIHTSVRDGLVSLARSLGLVVSVNAEPHKISYAIYM
SGGDVLLNVLSKCAGSKKFRPAPAAAFARECRGFYFELQELKEDDYYGIT
LSDDSDHQFLLANQVVVHN
Ligand information
>1um2 Chain D (length=7) Species:
4932
(Saccharomyces cerevisiae) [
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YVGSGER
Receptor-Ligand Complex Structure
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PDB
1um2
Protein splicing of yeast VMA1-derived endonuclease via thiazolidine intermediates.
Resolution
2.9 Å
Binding residue
(original residue number in PDB)
S284 N359 T361 E363 I717 T718 N737
Binding residue
(residue number reindexed from 1)
S1 N61 T63 E65 I399 T400 N419
Enzymatic activity
Catalytic site (original residue number in PDB)
S284 N359 T361 N362 K584 K686 G716 I717 N737
Catalytic site (residue number reindexed from 1)
S1 N61 T63 N64 K275 K368 G398 I399 N419
Enzyme Commision number
3.1.-.-
7.1.2.2
: H(+)-transporting two-sector ATPase.
Gene Ontology
Molecular Function
GO:0003677
DNA binding
GO:0004519
endonuclease activity
Biological Process
GO:0016539
intein-mediated protein splicing
GO:0030908
protein splicing
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Molecular Function
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Biological Process
External links
PDB
RCSB:1um2
,
PDBe:1um2
,
PDBj:1um2
PDBsum
1um2
PubMed
14646148
UniProt
P17255
|VATA_YEAST V-type proton ATPase catalytic subunit A (Gene Name=VMA1)
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