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2.9A crystal structure of methyl-isocitrate lyase from Burkholderia pseudomallei

A publication describing this structure is not available. The depositing authors are Seattle Structural Genomics Center for Infectious Disease (SSGCID)search

This crystal structure was determined using X-ray diffraction at a resolution of 2.9 Å and deposited in 2008.

The experimental data on which the structure is based was also deposited.

This PDB entry contains multiple copies of the structure of Methylisocitrate lyase.

The molecule has more than one probable quaternary state observed. For more details see the quaternary structure page.

The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):


Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A Methylisocitrate lyase B2H5R7 (11-308) (B2H5R7_BURPE)search Burkholderia pseudomallei 1655search 97% 298 97%
B Methylisocitrate lyase B2H5R7 (11-308) (B2H5R7_BURPE)search Burkholderia pseudomallei 1655search 97% 298 97%
C Methylisocitrate lyase B2H5R7 (11-308) (B2H5R7_BURPE)search Burkholderia pseudomallei 1655search 97% 298 97%
D Methylisocitrate lyase B2H5R7 (11-308) (B2H5R7_BURPE)search Burkholderia pseudomallei 1655search 97% 298 97%
E Methylisocitrate lyase B2H5R7 (11-308) (B2H5R7_BURPE)search Burkholderia pseudomallei 1655search 97% 298 97%
F Methylisocitrate lyase B2H5R7 (11-308) (B2H5R7_BURPE)search Burkholderia pseudomallei 1655search 97% 298 97%
G Methylisocitrate lyase B2H5R7 (11-308) (B2H5R7_BURPE)search Burkholderia pseudomallei 1655search 97% 298 97%
H Methylisocitrate lyase B2H5R7 (11-308) (B2H5R7_BURPE)search Burkholderia pseudomallei 1655search 97% 298 97%
I Methylisocitrate lyase B2H5R7 (11-308) (B2H5R7_BURPE)search Burkholderia pseudomallei 1655search 97% 298 97%
J Methylisocitrate lyase B2H5R7 (11-308) (B2H5R7_BURPE)search Burkholderia pseudomallei 1655search 97% 298 97%
K Methylisocitrate lyase B2H5R7 (11-308) (B2H5R7_BURPE)search Burkholderia pseudomallei 1655search 97% 298 97%
L Methylisocitrate lyase B2H5R7 (11-308) (B2H5R7_BURPE)search Burkholderia pseudomallei 1655search 97% 298 97%
M Methylisocitrate lyase B2H5R7 (11-308) (B2H5R7_BURPE)search Burkholderia pseudomallei 1655search 97% 298 97%
N Methylisocitrate lyase B2H5R7 (11-308) (B2H5R7_BURPE)search Burkholderia pseudomallei 1655search 97% 298 97%
O Methylisocitrate lyase B2H5R7 (11-308) (B2H5R7_BURPE)search Burkholderia pseudomallei 1655search 97% 298 97%
P Methylisocitrate lyase B2H5R7 (11-308) (B2H5R7_BURPE)search Burkholderia pseudomallei 1655search 97% 298 97%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
B2H5R7 (11 - 308) Methylisocitrate lyase Burkholderia pseudomallei 1655

Chain Structural classification (CATH) Sequence family (Pfam)
A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P (B2H5R7) Phosphoenolpyruvate-binding domainssearch PF13714: Phosphoenolpyruvate phosphomutasesearch

Chain ID Molecular function (GO) Biological process (GO)
A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P (B2H5R7) catalytic activitysearch lyase activitysearch methylisocitrate lyase activitysearch propionate catabolic process, 2-methylcitrate cyclesearch metabolic processsearch

Chain InterPro annotation
A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P Methylisocitrate lyasesearch Pyruvate/Phosphoenolpyruvate kinase-like domainsearch Isocitrate lyase/phosphorylmutase, conserved sitesearch