2E9X: Human GINS core complex
The crystal structure of human GINS core complex. Determined by X-ray diffraction at 2.3 Å resolution. Released 10 Apr 2007.
- Method
- X-ray diffraction
- Resolution
- 2.3 Å
- Organism
- Homo sapiens
- Chains
- 8
- Atoms
- 11,975
- Mol. weight
- 180.36 kDa
- Released
- 10 Apr 2007
Explore 2E9X in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
2E9X contains 83 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: 7 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 4-15 | 12 | |
| α-helix | 22-24 | 3 | |
| α-helix | 26-49 | 24 | |
| α-helix | 56-58 | 3 | |
| α-helix | 59-94 | 36 | |
| α-helix | 100-104 | 5 | |
| α-helix | 108-127 | 20 | |
Chain B: 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 | 142-144 | 3 | 4 |
| α-helix | 150-170 | 21 | |
Chain C: 13 helices, 5 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 999-1002 | 4 | |
| α-helix | 1007-1010 | 4 | |
| α-helix | 1022-1027 | 6 | |
| β-strand | 1031-1036 | 6 | 5 |
| β-strand | 1040 | 1 | 6 |
| α-helix | 1044-1046 | 3 | |
| β-strand | 1060 | 1 | 6 |
| β-strand | 1065-1069 | 5 | 5 |
| α-helix | 1070-1076 | 7 | |
| β-strand | 1084-1086 | 3 | 5 |
| α-helix | 1090-1092 | 3 | |
| α-helix | 1094-1102 | 9 | |
| α-helix | 1104-1106 | 3 | |
| α-helix | 1116-1122 | 7 | |
| α-helix | 1123-1126 | 4 | |
| α-helix | 1131-1153 | 23 | |
| α-helix | 1162-1165 | 4 | |
| α-helix | 1170-1190 | 21 | |
Chain D: 13 helices, 5 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 23-39 | 17 | |
| α-helix | 48-60 | 13 | |
| α-helix | 72-102 | 31 | |
| 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 | 151-153 | 3 | |
| α-helix | 158-161 | 4 | |
| α-helix | 163-165 | 3 | |
| β-strand | 170-175 | 6 | 4 |
| β-strand | 179-184 | 6 | 7 |
| α-helix | 190-192 | 3 | |
| β-strand | 194-198 | 5 | 7 |
| β-strand | 203-207 | 5 | 4 |
| α-helix | 208-217 | 10 | |
| β-strand | 220-222 | 3 | 4 |
Chain E: 7 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 4-15 | 12 | |
| α-helix | 17-19 | 3 | |
| α-helix | 22-24 | 3 | |
| α-helix | 26-51 | 26 | |
| α-helix | 59-94 | 36 | |
| α-helix | 100-103 | 4 | |
| α-helix | 108-126 | 19 | |
Chain F: 8 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 3-10 | 8 | |
| β-strand | 14-19 | 6 | 8 |
| β-strand | 23 | 1 | 9 |
| 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 | 61-63 | 3 | |
| α-helix | 68-80 | 13 | |
| α-helix | 84-87 | 4 | |
| α-helix | 92-103 | 12 | |
| α-helix | 110-137 | 28 | |
| β-strand | 142-144 | 3 | 11 |
| α-helix | 150-172 | 23 | |
Chain G: 13 helices, 5 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 7-10 | 4 | |
| α-helix | 22-27 | 6 | |
| β-strand | 31-36 | 6 | 12 |
| β-strand | 40 | 1 | 13 |
| α-helix | 59 | 1 | |
| β-strand | 60 | 1 | 13 |
| α-helix | 61 | 1 | |
| β-strand | 65-69 | 5 | 12 |
| α-helix | 70-76 | 7 | |
| β-strand | 84-86 | 3 | 12 |
| 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 | 170-191 | 22 | |
Chain H: 12 helices, 5 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 23-39 | 17 | |
| α-helix | 43-46 | 4 | |
| α-helix | 48-63 | 16 | |
| α-helix | 72-102 | 31 | |
| α-helix | 104-112 | 9 | |
| 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 | 14 |
| α-helix | 190-192 | 3 | |
| β-strand | 194-198 | 5 | 14 |
| β-strand | 203-207 | 5 | 11 |
| α-helix | 208-217 | 10 | |
| β-strand | 220-222 | 3 | 11 |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| DNA replication complex GINS protein PSF1 | A, E | protein | 149 | Homo sapiens | Q14691 (AlphaFold model) |
| DNA replication complex GINS protein PSF2 | B, F | protein | 185 | Homo sapiens | Q9Y248 (AlphaFold model) |
| GINS complex subunit 3 | C, G | protein | 219 | Homo sapiens | Q9BRX5 (AlphaFold model) |
| GINS complex subunit 4 | D, H | protein | 223 | Homo sapiens | Q9BRT9 (AlphaFold model) |
Sequence of entity 1 (A, E), FASTA
>2E9X_1 DNA replication complex GINS protein PSF1 (chains A, E)
MFCEKAMELIRELHRAPEGQLPAFNEDGLRQVLEEMKALYEQNQSDVNEAKSGGRSDLIP
TIKFRHCSLLRNRRCTVAYLYDRLLRIRALRWEYGSVLPNALRFHMAAEEMEWFNNYKRS
LATYMRSLGGDEGLDITQDMKPPKSLYIE
Sequence of entity 2 (B, F), FASTA
>2E9X_2 DNA replication complex GINS protein PSF2 (chains B, F)
MDAAEVEFLAEKELVTIIPNFSLDKIYLIGGDLGPFNPGLPVEVPLWLAINLKQRQKCRL
LPPEWMDVEKLEKMRDHERKEETFTPMPSPYYMELTKLLLNHASDNIPKADEIRTLVKDM
WDTRIAKLRVSADSFVRQQEAHAKLDNLTLMEINTSGTFLTQALNHMYKLRTNLQPLEST
QSQDF
Sequence of entity 3 (C, G), FASTA
>2E9X_3 GINS complex subunit 3 (chains C, G)
GPHMSEAYFRVESGALGPEENFLSLDDILMSHEKLPVRTETAMPRLGAFFLERSAGAETD
NAVPQGSKLELPLWLAKGLFDNKRRILSVELPKIYQEGWRTVFSADPNVVDLHKMGPHFY
GFGSQLLHFDSPENADISQSLLQTFIGRFRRIMDSSQNAYNEDTSALVARLDEMERGLFQ
TGQKGLNDFQCWEKGQASQITASNLVQNYKKRKFTDMED
Sequence of entity 4 (D, H), FASTA
>2E9X_4 GINS complex subunit 4 (chains D, H)
MTEEVDFLGQDSDGGSEEVVLTPAELIERLEQAWMNEKFAPELLESKPEIVECVMEQLEH
MEENLRRAKREDLKVSIHQMEMERIRYVLSSYLRCRLMKIEKFFPHVLEKEKTRPEGEPS
SLSPEELAFAREFMANTESYLKNVALKHMPPNLQKVDLFRAVPKPDLDSYVFLRVRERQE
NILVEPDTDEQRDYVIDLEKGSQHLIRYKTIAPLVASGAVQLI
Primary citation
Structure of the human GINS complex and its assembly and functional interface in replication initiation. Kamada, K., Kubota, Y., Arata, T. et al. Nat Struct Mol Biol (2007) 14:388-396. DOI 10.1038/nsmb1231 · PubMed
Other PDB entries of the same protein (UniProt Q14691 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 2Q9Q 2.36 Å, The crystal structure of full length human GINS 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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