Structure of PDB 1lwt Chain A

Receptor sequence
>1lwtA (length=448) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
CFAKGTNVLMADGSIECIENIEVGNKVMGKDGRPREVIKLPRGRETMYSV
VQKSQHRAHKSSREVPELLKFTCNATHELVVRTPRSVRRLSRTIKGVEYF
EVITFEMGQKKAPDGRIVELVKEVSKSYPISEGPERANELVESYRKASNK
AYFEWTIEARDLSLLGSHVRKATYQTYAPILYENDHFFDYMQKSKFHLTI
EGPKVLAYLLGLWIGDGLSDRATFSVDSRDTSLMERVTEYAEKLNLCAEY
KDRKAKTVNLYSKVVRGNGIRNNLNTENPLWDAIVGLGFLKDGVKNIPSF
LSTDNIGTRETFLAGLIDSDGYVTDEHGIKATIKTIHTSVRDGLVSLARS
LGLVVSVNAEPAKVDMNGTKHKISYAIYMSGGDVLLNVLSKCAGSKKFRP
APAAAFARECRGFYFELQELKEDDYYGITLSDDSDHQFLLANQVVVHN
3D structure
PDB1lwt Crystal structure of the intein homing endonuclease PI-SceI bound to its recognition sequence.
ChainA
Resolution3.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) C1 N76 T78 H79 K301 K403 G433 I434 N454
Catalytic site (residue number reindexed from 1) C1 N74 T76 H77 K295 K397 G427 I428 N448
Enzyme Commision number 3.1.-.-
7.1.2.2: H(+)-transporting two-sector ATPase.
Interaction with ligand
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:1lwt, PDBe:1lwt, PDBj:1lwt
PDBsum1lwt
PubMed12219083
UniProtP17255|VATA_YEAST V-type proton ATPase catalytic subunit A (Gene Name=VMA1)

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