3EIR: Putative ATP/GTP binding protein

Crystal structure of CHBP, a Cif Homologue from Burkholderia pseudomallei. Determined by X-ray diffraction at 2.1 Å resolution. Released 3 Feb 2009.

Method
X-ray diffraction
Resolution
2.1 Å
Organism
Burkholderia pseudomallei
Chains
2
Atoms
4,121
Mol. weight
62.62 kDa
Released
3 Feb 2009

Explore 3EIR in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3EIR contains 32 α-helices and 18 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 15 helices, 9 β-strands

ElementResiduesLengthSheet
α-helix81-9515
α-helix99-1057
α-helix114-1163
α-helix119-13214
α-helix136-1438
α-helix156-16813
β-strand18211
α-helix187-1915
β-strand199-20681
β-strand211-21771
β-strand22712
β-strand228-23031
β-strand23313
α-helix240-2412
β-strand24213
α-helix244-2518
β-strand25612
α-helix258-2647
α-helix267-2715
α-helix274-28512
α-helix291-2933
α-helix296-2983
β-strand305-31281
α-helix314-32512
Chain B: 17 helices, 9 β-strands
ElementResiduesLengthSheet
α-helix80-9516
α-helix99-1057
α-helix114-1163
α-helix119-13214
α-helix136-1427
α-helix151-1522
α-helix156-16813
β-strand18214
α-helix187-1937
β-strand199-20684
β-strand211-21774
α-helix218-2203
β-strand22715
β-strand228-23034
β-strand23316
α-helix240-2412
β-strand24216
α-helix244-2518
β-strand25615
α-helix258-2658
α-helix267-2715
α-helix274-28512
α-helix291-2933
α-helix296-2983
β-strand305-31284
α-helix314-32512

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Putative ATP/GTP binding proteinA, Bprotein281Burkholderia pseudomalleiQ63KH5 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>3EIR_1 Putative ATP/GTP binding protein (chains A, B)
GLPARSSSISNTNRTGENPMITPIISSNLGLKHRVTLRKATLASLMQSLSGESSNRVMWN
DRYDTLLIARDPREIKNAIEKSVTDFGGLENYKELTGGADPFALMTPVCGLSANNIFKLM
TEKDVPIDPTSIEYLENTSFAEHVNTLDSHKNYVVIVNDGRLGHKFLIDLPALTQGPRTA
YIIQSDLGGGALPAVRVEDWISRRGSDPVSLDELNQLLSKDFSKMPDDVQTRLLASILQI
DKDPHKVDIKKLHLDGKLRFASHEYDFRQFQRNAQYVAGLG

Primary citation

A bacterial type III effector family uses the papain-like hydrolytic activity to arrest the host cell cycle. Yao, Q., Cui, J., Zhu, Y. et al. Proc Natl Acad Sci U S A (2009) 106:3716-3721. DOI 10.1073/pnas.0900212106 · PubMed

Other PDB entries of the same protein (UniProt Q63KH5 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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