2IS4: UvrD-DNA-ADPNP ternary complex

Crystal structure of UvrD-DNA-ADPNP ternary complex. Determined by X-ray diffraction at 2.6 Å resolution. Released 9 Jan 2007.

Method
X-ray diffraction
Resolution
2.6 Å
Organism
Escherichia coli
Chains
4
Atoms
11,148
Mol. weight
172.63 kDa
Ligands
ANP, MG
Released
9 Jan 2007

Explore 2IS4 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2IS4 contains 80 α-helices and 48 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: 41 helices, 23 β-strands

ElementResiduesLengthSheet
α-helix3-86
α-helix12-187
β-strand25-2841
α-helix35-4814
α-helix54-563
β-strand57-6151
α-helix64-7714
β-strand86-8941
α-helix90-10011
α-helix102-1054
β-strand112-11432
α-helix116-12914
α-helix139-15214
α-helix165-18420
β-strand186-18832
α-helix189-20113
α-helix204-21310
β-strand216-21941
α-helix222-2243
α-helix227-23711
β-strand242-24761
α-helix249-2513
α-helix255-2573
α-helix263-2708
β-strand275-27841
β-strand28113
α-helix287-29711
β-strand30913
α-helix3171
β-strand318-32364
α-helix326-34116
α-helix347-3493
β-strand350-35454
α-helix357-3593
α-helix360-36910
β-strand374-37634
α-helix386-39813
α-helix404-4118
α-helix420-43112
α-helix439-4435
α-helix452-47221
α-helix477-48610
α-helix490-4934
α-helix502-51716
α-helix530-54112
β-strand554-55854
α-helix559-5624
β-strand567-57264
β-strand57615
β-strand578-57926
β-strand58216
α-helix583-5875
α-helix591-60313
β-strand606-615104
β-strand618-61927
β-strand624-62527
α-helix627-6282
β-strand62915
α-helix6301
α-helix631-6355
α-helix638-6403
β-strand641-64334
α-helix644-6452
α-helix652-6565
Chain B: 39 helices, 25 β-strands
ElementResiduesLengthSheet
α-helix3-75
α-helix12-187
β-strand25-2848
α-helix35-4814
α-helix54-563
β-strand57-6158
α-helix64-7815
β-strand8319
β-strand8519
β-strand86-8948
α-helix90-9910
α-helix1111
β-strand112-114310
α-helix116-12914
α-helix139-15113
α-helix170-18415
β-strand186-188310
α-helix189-20113
α-helix204-21310
β-strand216-21948
α-helix222-2243
α-helix227-23711
β-strand242-24768
α-helix249-2513
α-helix255-2573
α-helix263-2708
β-strand275-27848
β-strand281111
α-helix287-29711
β-strand309111
β-strand318-325812
α-helix326-34217
α-helix347-3493
β-strand350-354512
α-helix357-3593
α-helix360-3689
β-strand374-376312
α-helix382-3843
α-helix386-39914
α-helix404-4107
α-helix420-43314
α-helix437-4459
α-helix452-47120
α-helix477-48711
α-helix490-4956
α-helix504-51714
α-helix530-5356
β-strand554-558512
α-helix559-5624
β-strand567-572612
β-strand576113
β-strand578-579214
β-strand582114
α-helix583-5875
α-helix592-60413
β-strand606-6171212
β-strand618-619215
β-strand624-625215
α-helix627-6282
β-strand629113
α-helix6301
α-helix631-6344
α-helix638-6403
β-strand641-643312

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
25-MERC, DDNA26
DNA helicase IIA, Bprotein680Escherichia coliP03018 (AlphaFold model)
Sequence of entity 1 (C, D), FASTA
>2IS4_1 25-MER (chains C, D)
TCGAGCACTGCAGTGCTCGTTGTTTA
Sequence of entity 2 (A, B), FASTA
>2IS4_2 DNA helicase II (chains A, B)
MDVSYLLDSLNDKQREAVAAPRSNLLVLAGAGSGKTRVLVHRIAWLMSVENCSPYSIMAV
TFTNKAAAEMRHRIGQLMGTSQGGMWVGTFHGLAHRLLRAHHMDANLPQDFQILDSEDQL
RLLKRLIKAMNLDEKQWPPRQAMWYINSQKDEGLRPHHIQSYGNPVEQTWQKVYQAYQEA
CDRAGLVDFAELLLRAHELWLNKPHILQHYRERFTNILVDEFQDTNNIQYAWIRLLAGDT
GKVMIVGDDDQSIYGWRGAQVENIQRFLNDFPGAETIRLEQNYRSTSNILSAANALIENN
NGRLGKKLWTDGADGEPISLYCAFNELDEARFVVNRIKTWQDNGGALAECAILYRSNAQS
RVLEEALLQASMPYRIYGGMRFFERQEIKDALSYLRLIVNRNDDAAFERVVNTPTRGIGD
RTLDVVRQTSRDRQLTLWQACRELLQEKALAGRAASALQRFMELIDALAQETADMPLHVQ
TDRVIKDSGLRTMYEQEKGEKGQTRIENLEELVTATRQFSYNEEDEDLMPLQAFLSHAAL
EAGEGQADTWQDAVQLMTLHSAKGLEFPQVFIVGMEEGMFPSQMSLDEGGRLEEERRLAY
VGVTRAMQKLTLTYAETRRLYGKEVYHRPSRFIGELPEECVEEVRLRATVSRPVSHQRMG
TPMVENDSGYKLGQRVRHAK

Ligands and cofactors

IDNameFormulaCopies
ANPPhosphoaminophosphonic acid-adenylate esterC10 H17 N6 O12 P32
MGMagnesium ionMg2

Primary citation

UvrD helicase unwinds DNA one base pair at a time by a two-part power stroke. Lee, J.Y., Yang, W. Cell (2006) 127:1349-1360. DOI 10.1016/j.cell.2006.10.049 · PubMed

Other PDB entries of the same protein (UniProt P03018 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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