2Q9Q: Full length human GINS complex
The crystal structure of full length human GINS complex. Determined by X-ray diffraction at 2.36 Å resolution. Released 7 Aug 2007.
- Method
- X-ray diffraction
- Resolution
- 2.36 Å
- Organism
- Homo sapiens
- Chains
- 8
- Atoms
- 11,883
- Mol. weight
- 191.71 kDa
- Released
- 7 Aug 2007
Explore 2Q9Q in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
2Q9Q contains 84 α-helices and 36 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: 10 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 3-10 | 8 | |
| β-strand | 14-19 | 6 | 1 |
| β-strand | 23 | 1 | 2 |
| α-helix | 24-25 | 2 | |
| β-strand | 26-28 | 3 | 3 |
| β-strand | 31-33 | 3 | 3 |
| β-strand | 36 | 1 | 2 |
| β-strand | 42-45 | 4 | 1 |
| α-helix | 46-54 | 9 | |
| β-strand | 58-60 | 3 | 1 |
| α-helix | 61-63 | 3 | |
| α-helix | 68-80 | 13 | |
| α-helix | 84-87 | 4 | |
| α-helix | 92-103 | 12 | |
| α-helix | 104-106 | 3 | |
| α-helix | 110-137 | 28 | |
| β-strand | 143-144 | 2 | 4 |
| α-helix | 150-171 | 22 | |
Chain B: 13 helices, 5 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 23-39 | 17 | |
| α-helix | 48-64 | 17 | |
| α-helix | 73-102 | 30 | |
| α-helix | 104-112 | 9 | |
| α-helix | 114-115 | 2 | |
| α-helix | 119-120 | 2 | |
| α-helix | 124-144 | 21 | |
| α-helix | 146-148 | 3 | |
| α-helix | 158-161 | 4 | |
| α-helix | 163-165 | 3 | |
| β-strand | 170-175 | 6 | 4 |
| β-strand | 179-184 | 6 | 5 |
| α-helix | 190-192 | 3 | |
| β-strand | 194-198 | 5 | 5 |
| α-helix | 199 | 1 | |
| β-strand | 203-207 | 5 | 4 |
| α-helix | 208-217 | 10 | |
| β-strand | 220-221 | 2 | 4 |
Chain C: 6 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 4-14 | 11 | |
| α-helix | 22-24 | 3 | |
| α-helix | 26-51 | 26 | |
| α-helix | 59-93 | 35 | |
| α-helix | 100-103 | 4 | |
| α-helix | 108-128 | 21 | |
Chain D: 14 helices, 5 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 7-10 | 4 | |
| α-helix | 22-27 | 6 | |
| β-strand | 31-36 | 6 | 6 |
| β-strand | 40 | 1 | 7 |
| α-helix | 55-57 | 3 | |
| α-helix | 59 | 1 | |
| β-strand | 60 | 1 | 7 |
| α-helix | 61 | 1 | |
| β-strand | 65-69 | 5 | 6 |
| α-helix | 70-76 | 7 | |
| β-strand | 84-86 | 3 | 6 |
| α-helix | 90-92 | 3 | |
| α-helix | 94-102 | 9 | |
| α-helix | 104-106 | 3 | |
| α-helix | 116-123 | 8 | |
| α-helix | 124-126 | 3 | |
| α-helix | 131-153 | 23 | |
| α-helix | 162-165 | 4 | |
| α-helix | 170-189 | 20 | |
Chain E: 9 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 3-10 | 8 | |
| β-strand | 14-19 | 6 | 8 |
| β-strand | 23 | 1 | 9 |
| α-helix | 24-25 | 2 | |
| β-strand | 26-28 | 3 | 10 |
| β-strand | 31-33 | 3 | 10 |
| β-strand | 36 | 1 | 9 |
| β-strand | 42-45 | 4 | 8 |
| α-helix | 46-54 | 9 | |
| β-strand | 58-60 | 3 | 8 |
| α-helix | 68-80 | 13 | |
| α-helix | 84-87 | 4 | |
| α-helix | 92-103 | 12 | |
| α-helix | 104-106 | 3 | |
| α-helix | 110-137 | 28 | |
| β-strand | 142-144 | 3 | 11 |
| α-helix | 150-170 | 21 | |
Chain F: 13 helices, 5 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 23-39 | 17 | |
| α-helix | 43-46 | 4 | |
| α-helix | 48-64 | 17 | |
| α-helix | 73-102 | 30 | |
| α-helix | 104-112 | 9 | |
| α-helix | 114-115 | 2 | |
| α-helix | 119-120 | 2 | |
| α-helix | 124-144 | 21 | |
| α-helix | 146-148 | 3 | |
| α-helix | 158-161 | 4 | |
| α-helix | 163-165 | 3 | |
| β-strand | 170-175 | 6 | 11 |
| β-strand | 179-184 | 6 | 12 |
| α-helix | 190-192 | 3 | |
| β-strand | 194-198 | 5 | 12 |
| β-strand | 203-207 | 5 | 11 |
| α-helix | 212-217 | 6 | |
| β-strand | 220-221 | 2 | 11 |
Chain G: 6 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 5-14 | 10 | |
| α-helix | 22-24 | 3 | |
| α-helix | 26-50 | 25 | |
| α-helix | 59-93 | 35 | |
| α-helix | 100-103 | 4 | |
| α-helix | 108-125 | 18 | |
Chain H: 13 helices, 5 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 7-10 | 4 | |
| α-helix | 22-27 | 6 | |
| β-strand | 31-36 | 6 | 13 |
| β-strand | 40 | 1 | 14 |
| α-helix | 41-43 | 3 | |
| α-helix | 55-58 | 4 | |
| β-strand | 60 | 1 | 14 |
| β-strand | 65-69 | 5 | 13 |
| α-helix | 70-76 | 7 | |
| β-strand | 84-86 | 3 | 13 |
| α-helix | 90-92 | 3 | |
| α-helix | 94-102 | 9 | |
| α-helix | 104-106 | 3 | |
| α-helix | 116-123 | 8 | |
| α-helix | 124-126 | 3 | |
| α-helix | 131-153 | 23 | |
| α-helix | 162-165 | 4 | |
| α-helix | 170-190 | 21 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| DNA replication complex GINS protein PSF2 | A, E | protein | 191 | Homo sapiens | Q9Y248 (AlphaFold model) |
| GINS complex subunit 4 | B, F | protein | 223 | Homo sapiens | Q9BRT9 (AlphaFold model) |
| DNA replication complex GINS protein PSF1 | C, G | protein | 196 | Homo sapiens | Q14691 (AlphaFold model) |
| GINS complex subunit 3 | D, H | protein | 220 | Homo sapiens | Q9BRX5 (AlphaFold model) |
Sequence of entity 1 (A, E), FASTA
>2Q9Q_1 DNA replication complex GINS protein PSF2 (chains A, E)
GPLGSNMDAAEVEFLAEKELVTIIPNFSLDKIYLIGGDLGPFNPGLPVEVPLWLAINLKQ
RQKCRLLPPEWMDVEKLEKMRDHERKEETFTPMPSPYYMELTKLLLNHASDNIPKADEIR
TLVKDMWDTRIAKLRVSADSFVRQQEAHAKLDNLTLMEINTSGTFLTQALNHMYKLRTNL
QPLESTQSQDF
Sequence of entity 2 (B, F), FASTA
>2Q9Q_2 GINS complex subunit 4 (chains B, F)
MTEEVDFLGQDSDGGSEEVVLTPAELIERLEQAWMNEKFAPELLESKPEIVECVMEQLEH
MEENLRRAKREDLKVSIHQMEMERIRYVLSSYLRCRLMKIEKFFPHVLEKEKTRPEGEPS
SLSPEELAFAREFMANTESYLKNVALKHMPPNLQKVDLFRAVPKPDLDSYVFLRVRERQE
NILVEPDTDEQRDYVIDLEKGSQHLIRYKTIAPLVASGAVQLI
Sequence of entity 3 (C, G), FASTA
>2Q9Q_3 DNA replication complex GINS protein PSF1 (chains C, G)
MFCEKAMELIRELHRAPEGQLPAFNEDGLRQVLEEMKALYEQNQSDVNEAKSGGRSDLIP
TIKFRHCSLLRNRRCTVAYLYDRLLRIRALRWEYGSILPNALRFHMAAEEMEWFNNYKRS
LATYMRSLGGDEGLDITQDMKPPKSLYIEVRCLKDYGEFEVDDGTSVLLKKNSQHFLPRW
KCEQLIRQGVLEHILS
Sequence of entity 4 (D, H), FASTA
>2Q9Q_4 GINS complex subunit 3 (chains D, H)
GPGGGSEAYFRVESGALGPEENFLSLDDILMSHEKLPVRTETAMPRLGAFFLERSAGAET
DNAVPQGSKLELPLWLAKGLFDNKRRILSVELPKIYQEGWRTVFSADPNVVDLHKMGPHF
YGFGSQLLHFDSPENADISQSLLQTFIGRFRRIMDSSQNAYNEDTSALVARLDEMERGLF
QTGQKGLNDFQCWEKGQASQITASNLVQNYKKRKFTDMED
Primary citation
Crystal structure of the GINS complex and functional insights into its role in DNA replication. Chang, Y.P., Wang, G., Bermudez, V. et al. Proc Natl Acad Sci U S A (2007) 104:12685-12690. DOI 10.1073/pnas.0705558104 · PubMed
Other PDB entries of the same protein (UniProt Q9Y248 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 2E9X 2.3 Å, The crystal structure of human GINS core complex
- 9E2Z 2.6 Å, Cryo-EM structure of human CMG helicase stalled at G4-containing DNA template
- 7PLO 2.8 Å, H. sapiens replisome-CUL2/LRR1 complex
- 2EHO 3.0 Å, Crystal structure of human GINS complex
- 7PFO 3.2 Å, Core human replisome
- 6XTX 3.29 Å, CryoEM structure of human CMG bound to ATPgammaS and DNA
- 8B9D 3.4 Å, Human replisome bound by Pol Alpha
- 8OK2 4.1 Å, Bipartite interaction of TOPBP1 with the GINS complex
- 6XTY 6.77 Å, CryoEM structure of human CMG bound to AND-1 (CMGA)
Browse structure collections
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