3HPH: Closed tetramer of Visna virus integrase

Closed tetramer of Visna virus integrase (residues 1-219) in complex with LEDGF IBD. Determined by X-ray diffraction at 2.64 Å resolution. Released 28 Jul 2009.

Method
X-ray diffraction
Resolution
2.64 Å
Organisms
Maedi visna virus, Homo sapiens
Chains
8
Atoms
8,778
Mol. weight
145.23 kDa
Ligands
ZN, PO4
Released
28 Jul 2009

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

Secondary structure: helices and β-sheets

3HPH contains 77 α-helices and 24 β-strands across 8 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: 12 helices, 5 β-strands

ElementResiduesLengthSheet
α-helix5-1511
α-helix19-257
α-helix30-378
β-strand62-7091
β-strand73-8081
β-strand86-9161
α-helix96-11015
β-strand114-11741
α-helix121-1244
α-helix126-13510
β-strand138-14141
α-helix143-1453
α-helix147-16721
α-helix168-1703
α-helix174-18310
α-helix184-1885
α-helix197-21216
Chain B: 11 helices, 7 β-strands
ElementResiduesLengthSheet
α-helix5-1511
α-helix19-268
α-helix30-389
β-strand62-7092
β-strand73-8082
β-strand86-9162
α-helix96-11015
β-strand114-11742
α-helix121-1244
α-helix126-13510
β-strand138-14142
α-helix152-16716
α-helix168-1703
α-helix174-18310
α-helix184-1885
β-strand19113
β-strand19513
α-helix197-21216
Chain C: 11 helices, 7 β-strands
ElementResiduesLengthSheet
α-helix5-1511
α-helix19-268
α-helix30-389
β-strand62-7094
β-strand73-8084
β-strand86-9164
α-helix96-11015
β-strand114-11854
α-helix121-1244
α-helix126-13510
β-strand138-14254
α-helix152-16716
α-helix168-1703
α-helix174-18310
α-helix184-1885
β-strand19115
β-strand19515
α-helix197-21216
Chain D: 12 helices, 5 β-strands
ElementResiduesLengthSheet
α-helix5-1511
α-helix19-257
α-helix30-378
β-strand62-7096
β-strand73-8086
β-strand86-9166
α-helix96-11015
β-strand114-11746
α-helix121-1244
α-helix126-1349
β-strand138-14146
α-helix143-1453
α-helix147-16721
α-helix168-1703
α-helix174-18310
α-helix184-1885
α-helix197-21317
Chains E and H: 9 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix349-36214
α-helix365-3673
α-helix370-38213
α-helix387-3904
α-helix391-3933
α-helix394-4029
α-helix403-4053
α-helix410-42718
α-helix435-4395
Chain F: 6 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix353-36210
α-helix365-3673
α-helix370-3778
α-helix397-4026
α-helix403-4053
α-helix410-42314
Chain G: 7 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix354-3629
α-helix365-3673
α-helix370-3778
α-helix378-3803
α-helix397-4026
α-helix403-4053
α-helix410-41910

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
IntegraseA, B, C, Dprotein219Maedi visna virusP35956
PC4 and SFRS1-interacting proteinE, F, G, Hprotein94Homo sapiensO75475 (AlphaFold model)
Sequence of entity 1 (A, B, C, D), FASTA
>3HPH_1 Integrase (chains A, B, C, D)
MVENIPLAEEEHNKWHQDAVSLHLEFGIPRTAAEDIVQQCDVCQENKMPSTLRGSNKRGI
DHWQVDYTHYEDKIILVWVETNSGLIYAERVKGETGQEFRVQTMKWYAMFAPKSLQSDNG
PAFVAESTQLLMKYLGIEHTTGIPWNPQSQALVERTHQTLKNTLEKLIPMFNAFESALAG
TLITLNIKRKGGLGTSPMDIFIFNKEQQRIQQQSKSKQE
Sequence of entity 2 (E, F, G, H), FASTA
>3HPH_2 PC4 and SFRS1-interacting protein (chains E, F, G, H)
MDSRLQRIHAEIKNSLKIDNLDVNRCIEALDELASLQVTMQQAQKHTEMITTLKKIRRFK
VSQVIMEKSTMLYNKFKNMFLVGEGDSVLEVLFQ

Ligands and cofactors

IDNameFormulaCopies
ZNZinc ionZn4
PO4Phosphate ionO4 P3

Water and common crystallization additives (GOL) are not listed.

Primary citation

Structural basis for functional tetramerization of lentiviral integrase. Hare, S., Di Nunzio, F., Labeja, A. et al. PLoS Pathog (2009) 5:e1000515-e1000515. DOI 10.1371/journal.ppat.1000515 · PubMed

Other PDB entries of the same protein (UniProt P35956), best resolution first:

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