PDB entry 3bs8

View 3bs8 on RCSB PDB site
Description: Crystal structure of Glutamate 1-Semialdehyde Aminotransferase complexed with pyridoxamine-5'-phosphate From Bacillus subtilis
Class: isomerase
Keywords: glutamate-1-semialdehyde 2,1-aminotransferase, porphyrin biosynthesis, Isomerase, Pyridoxal phosphate
Deposited on 2007-12-22, released 2008-12-23
The last revision prior to the SCOPe 2.07 freeze date was dated 2010-11-24, with a file datestamp of 2010-11-19.
Experiment type: XRAY
Resolution: 2.3 Å
R-factor: 0.195
AEROSPACI score: 0.38 (click here for full SPACI score report)

Chains and heterogens:

  • Chain 'A':
    Compound: Glutamate-1-semialdehyde 2,1-aminomutase
    Species: Bacillus subtilis [TaxId:1423]
    Database cross-references and differences (RAF-indexed):
    • Uniprot P30949 (8-437)
      • engineered mutation (328)
      • engineered mutation (347)
      • engineered mutation (349)
      • engineered mutation (381)
    Domains in SCOPe 2.07: d3bs8a_
  • Heterogens: PMP, HOH

PDB Chain Sequences:

  • Chain 'A':
    Sequence, based on SEQRES records: (download) 
    >3bs8A (A:)
mghhhhhhmrsyeksktafkeaqklmpggvnspvrafksvdmdpifmergkgskifdidg
neyidyvlswgplilghtndrvveslkkvaeygtsfgaptevenelaklvidrvpsveiv
rmvssgteatmsalrlargytgrnkilkfegcyhghgdsllikagsgvatlglpdspgvp
egiakntitvpyndlesvklafqqfgediagvivepvagnmgvvppqegflqglrditeq
ygsllifdevmtgfrvdyncaqgyfgvtpdltclgkviggglpvgayggkaeimeqiaps
gpiyqagtlsgnplamtagletlkqltpdsyknfikkgdrleegiskaaeahgiphtfnr
agsmigffftnepvinyetakasdlklfasyykgmanegvflppsqfeglflstahtded
ientiqaaekvfaeisrr

    Sequence, based on observed residues (ATOM records): (download) 
    >3bs8A (A:)
mrsyeksktafkeaqklmpggvnspvrafksvdmdpifmergkgskifdidgneyidyvl
swgplilghtndrvveslkkvaeygtsfgaptevenelaklvidrvpsveivrmvssgte
atmsalrlargytgrnkilkfegcyhghgdsllikagsgvatlglpdspgvpegiaknti
tvpyndlesvklafqqfgediagvivepvagnmgvvppqegflqglrditeqygsllifd
evmtgfrvdyncaqgyfgvtpdltclgkviggglpvgayggkaeimeqiapsgpiyqagt
lsgnplamtagletlkqltpdsyknfikkgdrleegiskaaeahgiphtfnragsmigff
ftnepvinyetakasdlklfasyykgmanegvflppsqfeglflstahtdedientiqaa
ekvfaeisrr