2EHO: Human GINS complex

Crystal structure of human GINS complex. Determined by X-ray diffraction at 3.0 Å resolution. Released 19 Jun 2007.

Method: X-ray diffraction
Resolution: 3.0 Å
Organism: Homo sapiens
Chains: 12
Atoms: 16,937
Mol. weight: 270.09 kDa
Released: 19 Jun 2007

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

Secondary structure: helices and β-sheets

2EHO contains 106 α-helices and 52 β-strands across 12 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, 4 β-strands

Element	Residues	Length	Sheet
α-helix	23-39	17
α-helix	44-46	3
α-helix	48-65	18
α-helix	72-102	31
α-helix	105-108	4
α-helix	124-141	18
α-helix	142-146	5
α-helix	158-161	4
α-helix	163-165	3
β-strand	170	1	1
β-strand	173	1	2
β-strand	204	1	2
β-strand	207	1	1
α-helix	208-211	4

Chain B: 7 helices, 0 β-strands

Element	Residues	Length
α-helix	4-14	11
α-helix	22-24	3
α-helix	26-51	26
α-helix	59-94	36
α-helix	98-99	2
α-helix	100-103	4
α-helix	108-125	18

Chain C: 10 helices, 9 β-strands

Element	Residues	Length	Sheet
α-helix	3-10	8
β-strand	14-19	6	3
β-strand	23	1	4
β-strand	26-28	3	5
β-strand	31-33	3	5
β-strand	36	1	4
β-strand	37	1	6
β-strand	40	1	6
β-strand	42-45	4	3
α-helix	46-54	9
β-strand	58-61	4	3
α-helix	62-63	2
α-helix	68-71	4
α-helix	74-78	5
α-helix	84-87	4
α-helix	92-102	11
α-helix	104-106	3
α-helix	110-137	28
α-helix	157-170	14

Chain D: 10 helices, 5 β-strands

Element	Residues	Length	Sheet
α-helix	22-27	6
β-strand	33-36	4	7
β-strand	40-41	2	8
β-strand	59-60	2	8
β-strand	65-67	3	7
α-helix	70-76	7
β-strand	84-86	3	7
α-helix	96-102	7
α-helix	104-106	3
α-helix	116-122	7
α-helix	131-138	8
α-helix	146-153	8
α-helix	161-164	4
α-helix	165-167	3
α-helix	172-182	11

Chain E: 9 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	23-39	17
α-helix	48-63	16
α-helix	73-112	40
α-helix	124-144	21
α-helix	146-148	3
α-helix	150	1
α-helix	158-161	4
α-helix	163-165	3
β-strand	170-174	5	9
β-strand	179-184	6	10
β-strand	194-198	5	10
β-strand	203-207	5	9
α-helix	208-211	4

Chain F: 5 helices, 0 β-strands

Element	Residues	Length
α-helix	4-15	12
α-helix	26-48	23
α-helix	59-93	35
α-helix	100-104	5
α-helix	108-126	19

Chain G: 7 helices, 8 β-strands

Element	Residues	Length	Sheet
α-helix	3-10	8
β-strand	14-17	4	11
β-strand	23	1	12
β-strand	26-27	2	13
β-strand	32-33	2	13
β-strand	36	1	12
β-strand	42-45	4	11
α-helix	46-53	8
β-strand	60	1	11
α-helix	68-81	14
α-helix	92-101	10
α-helix	110-137	28
β-strand	143-144	2	9
α-helix	150-153	4
α-helix	157-170	14

Chain H: 12 helices, 5 β-strands

Element	Residues	Length	Sheet
α-helix	7-10	4
α-helix	22-27	6
β-strand	31-36	6	14
β-strand	40	1	15
α-helix	44-46	3
β-strand	60	1	15
β-strand	65-69	5	14
α-helix	70-76	7
β-strand	84-86	3	14
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	159-165	7
α-helix	170-189	20

4 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
GINS complex subunit 4	A, E, I	protein	203	Homo sapiens	Q9BRT9 (AlphaFold model)
DNA replication complex GINS protein PSF1	B, F, J	protein	152	Homo sapiens	Q14691 (AlphaFold model)
DNA replication complex GINS protein PSF2	C, G, K	protein	186	Homo sapiens	Q9Y248 (AlphaFold model)
GINS complex subunit 3	D, H, L	protein	216	Homo sapiens	Q9BRX5 (AlphaFold model)

Sequence of entity 1 (A, E, I), FASTA

>2EHO_1 GINS complex subunit 4 (chains A, E, I)
DSDGGSEEVVLTPAELIERLEQAWMNEKFAPELLESKPEIVECVMEQLEHMEENLRRAKR
EDLKVSIHQMEMERIRYVLSSYLRCRLMKIEKFFPHVLEKEKTRPEGEPSSLSPEELAFA
REFMANTESYLKNVALKHMPPNLQKVDLFRAVPKPDLDSYVFLRVRERQENILVEPDTDE
QRDYVIDLEKGSQHLIRYKTIAP

Sequence of entity 2 (B, F, J), FASTA

>2EHO_2 DNA replication complex GINS protein PSF1 (chains B, F, J)
MMFCEKAMELIRELHRAPEGQLPAFNEDGLRQVLEEMKALYEQNQSDVNEAKSGGRSDLI
PTIKFRHCSLLRNRRCTVAYLYDRLLRIRALRWEYGSILPNALRFHMAAEEMEWFNNYKR
SLATYMRSLGGDEGLDITQDMKPPKSLYIEVR

Sequence of entity 3 (C, G, K), FASTA

>2EHO_3 DNA replication complex GINS protein PSF2 (chains C, G, K)
MMDAAEVEFLAEKELVTIIPNFSLDKIYLIGGDLGPFNPGLPVEVPLWLAINLKQRQKCR
LLPPEWMDVEKLEKMRDHERKEETFTPMPSPYYMELTKLLLNHASDNIPKADEIRTLVKD
MWDTRIAKLRVSADSFVRQQEAHAKLDNLTLMEINTSGTFLTQALNHMYKLRTNLQPLES
TQSQDF

Sequence of entity 4 (D, H, L), FASTA

>2EHO_4 GINS complex subunit 3 (chains D, H, L)
MSEAYFRVESGALGPEENFLSLDDILMSHEKLPVRTETAMPRLGAFFLERSAGAETDNAV
PQGSKLELPLWLAKGLFDNKRRILSVELPKIYQEGWRTVFSADPNVVDLHKMGPHFYGFG
SQLLHFDSPENADISQSLLQTFIGRFRRIMDSSQNAYNEDTSALVARLDEMERGLFQTGQ
KGLNDFQCWEKGQASQITASNLVQNYKKRKFTDMED

Primary citation

Crystal structure of the human GINS complex. Choi, J.M., Lim, H.S., Kim, J.J. et al. Genes Dev (2007) 21:1316-1321. DOI 10.1101/gad.1548107 · PubMed

Other PDB entries of the same protein (UniProt Q9BRT9 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2E9X 2.3 Å, The crystal structure of human GINS core complex
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
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)

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