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MolNFT v1 · #160759 · protein

Structure of CTF4 trimer in complex with two cmg helicases

6PTN · DNA polymerase alpha-binding protein: “Structure of CTF4 trimer in complex with two cmg helicases”. Electron microscopy, 1 ligand (ATP), 20 pockets (best druggability 0.89). MolNFT v1 #160759 on GenesisL1: 3D structure, binding…

PDB
6PTN
Type
protein
Length
11,517 residues
Chains
25
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
DNA polymerase alpha-binding protein; DNA replication complex gins protein PSF1; DNA…
EC
3.6.4.12
UniProt
Q01454, Q12488, P40359, Q12146, Q03406, Q08032, P29469, P24279, P30665, P29496, P53091, P38132
Ligands
ATP
Pockets
20 · best druggability 0.89

Structure

electron microscopy · 13 distinct chains · 32% helix, 13% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
E, GDNA polymerase alpha-binding proteinprotein42425% helix, 30% strandQ01454
FDNA polymerase alpha-binding proteinprotein43125% helix, 29% strandQ01454
a, ADNA replication complex gins protein PSF1protein20851% helix, 5% strandQ12488
b, BDNA replication complex gins protein PSF2protein18141% helix, 7% strandP40359
c, CDNA replication complex gins protein PSF3protein15947% helix, 6% strandQ12146
d, DDNA replication complex gins protein SLD5protein23451% helix, 5% strandQ03406
h, HCell division control protein 45protein55342% helix, 8% strandQ08032
i, 2DNA replication licensing factor MCM2 (EC 3.6.4.12)protein63431% helix, 7% strandP29469
j, 3DNA replication licensing factor MCM3 (EC 3.6.4.12)protein59429% helix, 14% strandP24279
k, 4DNA replication licensing factor MCM4 (EC 3.6.4.12)protein68230% helix, 12% strandP30665
l, 5Minichromosome maintenance protein 5 (EC 3.6.4.12)protein59731% helix, 13% strandP29496
m, 6DNA replication licensing factor MCM6 (EC 3.6.4.12)protein61429% helix, 10% strandP53091
n, 7DNA replication licensing factor MCM7 (EC 3.6.4.12)protein66327% helix, 10% strandP38132

Ligands and binding sites

  • ATP · Adenosine-5'-triphosphate · ligand · 6 copies · chains i, m, j, l, 2, 6, 3, 5

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
18860.890.92126empty
210350.880.89140empty
37790.870.9091empty
410030.870.89115ATP
511260.870.88131empty

Interfaces

57 interfaces between chains.

  • k–m · 3851 Ų buried · 25 hydrogen bonds · protein-protein
  • 4–6 · 3849 Ų buried · 25 hydrogen bonds · protein-protein
  • j–l · 3691 Ų buried · 27 hydrogen bonds · protein-protein
  • 3–5 · 3688 Ų buried · 27 hydrogen bonds · protein-protein
  • i–m · 3536 Ų buried · 22 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

  • 6PTN · Structure of Ctf4 trimer in complex with two CMG helicases · the same entry in another collection · chain l against l, TM-score 1.00

Analyse

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