Structure of PDB 1um2 Chain B

Receptor sequence
>1um2B (length=419) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
SFAKGTNVLMADGSIECIENIEVGNKVMGKDGRPREVIKLPRGRETMYSV
VQKELLKFTCNATNELVVRTPRSVRRLSRTIKGVEYFEVITFEMGQKKAP
DGRIVELVKEVSKSYPISEGPERANELVESYRKASNKAYFEWTIEARDLS
LLGSHVRKATYQTYAPILYENDHFFDYMQKSKFHLTIEGPKVLAYLLGLW
IGDGLSDRATFSVDSRDTSLMERVTEYAEKLNLCAEYKDRKEPQVAKTVN
LYSLNTENPLWDAIVGLGFLKDGVKNIPSFLSTDNIGTRETFLAGLIDSD
GYVTDEHGIKATIKTIHTSVRDGLVSLARSLGLVVSVNAEPHKISYAIYM
SGGDVLLNVLSKCAGSKKFRPAPAAAFARECRGFYFELQELKEDDYYGIT
LSDDSDHQFLLANQVVVHN
3D structure
PDB1um2 Protein splicing of yeast VMA1-derived endonuclease via thiazolidine intermediates.
ChainB
Resolution2.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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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.
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 peptide B S284 N359 T361 E363 I717 T718 N737 S1 N61 T63 E65 I399 T400 N419
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
PDBsum1um2
PubMed14646148
UniProtP17255|VATA_YEAST V-type proton ATPase catalytic subunit A (Gene Name=VMA1)

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