4QMG: PDB entry 4QMG

The Structure of MTDH-SND1 Complex Reveals Novel Cancer-Promoting Interactions. Determined by X-ray diffraction at 2.7 Å resolution. Released 8 Oct 2014.

Method
X-ray diffraction
Resolution
2.7 Å
Organism
Homo sapiens
Chains
10
Atoms
13,224
Mol. weight
208.07 kDa
Ligands
CS
Released
8 Oct 2014

Explore 4QMG in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4QMG contains 82 α-helices and 101 β-strands across 6 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: 16 helices, 20 β-strands

ElementResiduesLengthSheet
β-strand20-2781
α-helix29-313
β-strand33-3641
α-helix44-452
β-strand46-5161
β-strand54-5632
α-helix57-604
β-strand6113
β-strand7313
α-helix75-762
α-helix79-9012
β-strand94-10291
β-strand108-11471
β-strand121-12221
α-helix123-1297
β-strand133-13532
α-helix144-15916
α-helix162-1643
α-helix170-1723
β-strand17714
α-helix183-1886
β-strand195-204104
β-strand207-21264
β-strand217-22374
β-strand226-22725
β-strand23116
β-strand24116
α-helix2421
α-helix245-25612
β-strand260-269104
β-strand272-27874
α-helix284-2918
β-strand295-29625
α-helix301-3033
α-helix308-32013
α-helix324-3263
Chain B: 15 helices, 20 β-strands
ElementResiduesLengthSheet
β-strand19-2797
α-helix29-313
β-strand32-3657
α-helix43-453
β-strand46-5167
β-strand54-5638
α-helix57-604
β-strand6119
β-strand7319
α-helix74-763
α-helix79-9012
β-strand94-10297
β-strand108-11477
β-strand121-12227
α-helix123-1297
β-strand133-13538
α-helix146-15813
α-helix162-1643
α-helix170-1723
β-strand177110
α-helix183-1897
β-strand195-2041010
β-strand207-212610
β-strand217-223710
β-strand226-227211
β-strand231112
β-strand241112
α-helix2421
α-helix245-25612
β-strand260-2691010
β-strand272-278710
α-helix284-2918
β-strand295-296211
α-helix308-31912
α-helix324-3263
Chain C: 17 helices, 20 β-strands
ElementResiduesLengthSheet
β-strand20-27813
α-helix29-313
β-strand33-36413
α-helix44-452
β-strand46-51613
β-strand54-55214
α-helix57-604
β-strand61115
β-strand73115
α-helix75-762
α-helix79-9012
β-strand94-102913
β-strand108-114713
β-strand121-122213
α-helix123-1297
β-strand134-135214
α-helix141-1422
α-helix144-15916
α-helix162-1643
α-helix170-1723
β-strand177116
α-helix183-1897
β-strand195-2041016
β-strand207-212616
β-strand217-223716
β-strand226-227217
β-strand231-232218
β-strand240-241218
α-helix2421
α-helix245-25612
β-strand260-2691016
β-strand272-278716
α-helix284-2907
β-strand295-296217
α-helix301-3033
α-helix308-32013
α-helix324-3263
Chain D: 18 helices, 20 β-strands
ElementResiduesLengthSheet
β-strand19-27919
α-helix29-313
β-strand33-36419
α-helix43-453
β-strand46-51619
β-strand54-55220
α-helix57-604
β-strand61121
α-helix62-643
α-helix721
β-strand73121
α-helix74-763
α-helix80-9011
β-strand94-102919
β-strand108-114719
β-strand121-122219
α-helix123-1297
β-strand134-135220
α-helix1361
α-helix144-15815
α-helix162-1643
α-helix170-1723
β-strand177122
α-helix183-1886
β-strand195-2041022
β-strand207-212622
β-strand217-223722
β-strand226-227223
β-strand231124
β-strand241124
α-helix2421
α-helix245-25612
β-strand260-2691022
β-strand272-278722
α-helix284-2907
β-strand295-296223
α-helix308-31912
α-helix324-3263
Chain E: 15 helices, 21 β-strands
ElementResiduesLengthSheet
β-strand20-27825
α-helix29-313
β-strand32-36525
α-helix43-453
β-strand46-51625
β-strand54-56326
α-helix57-604
β-strand61127
β-strand73127
α-helix75-762
α-helix79-9012
β-strand94-101825
β-strand108-114725
β-strand121-122225
α-helix123-1297
β-strand133-135326
α-helix144-15916
α-helix162-1643
α-helix170-1723
β-strand177128
α-helix183-1886
β-strand195-2041028
β-strand207-212628
β-strand217-223728
β-strand226-227229
β-strand231-232230
β-strand240-241230
α-helix2421
α-helix245-25612
β-strand260-2691028
β-strand272-279828
β-strand282-283228
α-helix284-2918
β-strand295-296229
α-helix308-32013
α-helix324-3263
Chain G: 1 helix, 0 β-strands
ElementResiduesLengthSheet
α-helix395-3973

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Staphylococcal nuclease domain-containing protein 1A, B, C, D, Eprotein325Homo sapiensQ7KZF4 (AlphaFold model)
Protein LYRICF, G, H, I, Jprotein43Homo sapiensQ86UE4 (AlphaFold model)
Sequence of entity 1 (A, B, C, D, E), FASTA
>4QMG_1 Staphylococcal nuclease domain-containing protein 1 (chains A, B, C, D, E)
MVPTVQRGIIKMVLSGCAIIVRGQPRGGPPPERQINLSNIRAGNLARRAAATQPDAKDTP
DEPWAFPAREFLRKKLIGKEVCFTIENKTPQGREYGMIYLGKDTNGENIAESLVAEGLAT
RREGMRANNPEQNRLSECEEQAKAAKKGMWSEGNGSHTIRDLKYTIENPRHFVDSHHQKP
VNAIIEHVRDGSVVRALLLPDYYLVTVMLSGIKCPTFRREADGSETPEPFAAEAKFFTES
RLLQRDVQIILESCHNQNILGTILHPNGNITELLLKEGFARCVDWSIAVYTRGAEKLRAA
ERFAKERRLRIWRDYVAPTANLDQK
Sequence of entity 2 (F, G, H, I, J), FASTA
>4QMG_2 Protein LYRIC (chains F, G, H, I, J)
STGNASDSSSDSSSSEGDGTVSSADPNSDWNAPAEEWGNWVDE

Ligands and cofactors

IDNameFormulaCopies
CSCesium ionCs5

Water and common crystallization additives (GOL, SO4) are not listed.

Primary citation

Structural Insights into the Tumor-Promoting Function of the MTDH-SND1 Complex. Guo, F., Wan, L., Zheng, A. et al. Cell Rep (2014) 8:1704-1713. DOI 10.1016/j.celrep.2014.08.033 · PubMed

Other PDB entries of the same protein (UniProt Q7KZF4 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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