2ZHX: Uracil-DNA glycosylase

Crystal structure of Uracil-DNA Glycosylase from Mycobacterium tuberculosis in complex with a proteinaceous inhibitor. Determined by X-ray diffraction at 3.1 Å resolution. Released 20 May 2008.

Method
X-ray diffraction
Resolution
3.1 Å
Organisms
Mycobacterium tuberculosis H37Rv, Bacillus phage PBS2
Chains
14
Atoms
16,840
Mol. weight
247.07 kDa
Released
20 May 2008

Explore 2ZHX in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2ZHX contains 121 α-helices and 80 β-strands across 14 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, 4 β-strands

ElementResiduesLengthSheet
α-helix6-83
α-helix14-185
α-helix19-213
α-helix22-3716
α-helix46-483
α-helix51-544
β-strand62-6541
α-helix69-702
α-helix92-10413
α-helix107-1104
α-helix116-1194
β-strand123-12421
α-helix145-15814
β-strand163-16861
α-helix170-1734
β-strand184-18961
α-helix197-1993
α-helix206-21611
α-helix220-2223
Chain B: 2 helices, 5 β-strands
ElementResiduesLengthSheet
α-helix5-128
β-strand18-2472
α-helix26-338
β-strand41-4882
β-strand53-6082
β-strand67-7372
β-strand79-8352
Chain C: 15 helices, 8 β-strands
ElementResiduesLengthSheet
α-helix6-94
α-helix14-185
α-helix19-213
α-helix22-3716
α-helix46-483
α-helix51-544
β-strand62-6433
β-strand6614
α-helix92-10413
α-helix107-1104
α-helix116-1194
β-strand123-12423
β-strand12714
β-strand13315
β-strand13615
α-helix145-15814
β-strand163-16863
α-helix170-1734
β-strand184-18963
α-helix194-1963
α-helix197-2015
α-helix206-21611
α-helix220-2223
Chain D: 2 helices, 5 β-strands
ElementResiduesLengthSheet
α-helix6-127
β-strand18-2476
α-helix26-338
β-strand41-4886
β-strand53-5976
β-strand67-7376
β-strand79-8356
Chain E: 15 helices, 6 β-strands
ElementResiduesLengthSheet
α-helix6-94
α-helix14-185
α-helix19-213
α-helix22-3716
α-helix46-483
α-helix51-544
β-strand62-6547
β-strand6618
α-helix92-10413
α-helix107-1104
α-helix116-1194
β-strand123-12427
β-strand12718
α-helix145-15814
β-strand163-16867
α-helix170-1734
β-strand184-18967
α-helix194-1963
α-helix197-2015
α-helix206-21611
α-helix220-2223
Chain F: 2 helices, 5 β-strands
ElementResiduesLengthSheet
α-helix6-127
β-strand20-2459
α-helix26-338
β-strand41-4889
β-strand53-6089
β-strand67-7379
β-strand79-8359
Chain G: 15 helices, 4 β-strands
ElementResiduesLengthSheet
α-helix6-94
α-helix14-185
α-helix19-213
α-helix22-3817
α-helix46-483
α-helix51-544
β-strand62-65410
α-helix92-10413
α-helix107-1104
α-helix116-1194
β-strand123-124210
α-helix145-15814
β-strand163-168610
α-helix170-1734
β-strand184-189610
α-helix194-1963
α-helix197-2015
α-helix206-21611
α-helix220-2223
Chain H: 2 helices, 5 β-strands
ElementResiduesLengthSheet
α-helix5-117
β-strand20-24511
α-helix26-338
β-strand41-48811
β-strand53-59711
β-strand67-73711
β-strand79-83511

6 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Uracil-DNA glycosylaseA, C, E, G, I, K, Mprotein238Mycobacterium tuberculosis H37RvP9WFQ9 (AlphaFold model)
Uracil-DNA glycosylase inhibitorB, D, F, H, J, L, Nprotein84Bacillus phage PBS2P14739 (AlphaFold model)
Sequence of entity 1 (A, C, E, G, I, K, M), FASTA
>2ZHX_1 Uracil-DNA glycosylase (chains A, C, E, G, I, K, M)
MHHHHHHGMASMTARPLSELVERGWAAALEPVADQVAHMGQFLRAEIAAGRRYLPAGSNV
LRAFTFPFDNVRVLIVGQDPYPTPGHAVGLSFSVAPDVRPWPRSLANIFDEYTADLGYPL
PSNGDLTPWAQRGVLLLNRVLTVRPSNPASHRGKGWEAVTECAIRALAARAAPLVAILWG
RDASTLKPMLAAGNCVAIESPHPSPLSASRGFFGSRPFSRANELLVGMGAEPIDWRLP
Sequence of entity 2 (B, D, F, H, J, L, N), FASTA
>2ZHX_2 Uracil-DNA glycosylase inhibitor (chains B, D, F, H, J, L, N)
MTNLSDIIEKETGKQLVIQESILMLPEEVEEVIGNKPESDILVHTAYDESTDENVMLLTS
DAPEYKPWALVIQDSNGENKIKML

Primary citation

Unique features of the structure and interactions of mycobacterial uracil-DNA glycosylase: structure of a complex of the Mycobacterium tuberculosis enzyme in comparison with those from other sources. Kaushal, P.S., Talawar, R.K., Krishna, P.D.V. et al. Acta Crystallogr D Biol Crystallogr (2008) 64:551-560. DOI 10.1107/S090744490800512X · PubMed

Other PDB entries of the same protein (UniProt P9WFQ9 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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