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Structure of CTF4 trimer in complex with one cmg helicase

Analyse Structure of CTF4 trimer in complex with one cmg helicase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6PTJ
Type: protein
Length: 4,280 residues
Chains: 14
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: DNA replication complex gins protein PSF1; DNA replication complex gins protein PSF2; DNA…
EC: 3.6.4.12
UniProt: Q12488, P40359, Q12146, Q03406, Q08032, P29469, P24279, P30665, P29496, P53091, P38132, Q01454
Pockets: 20 · best druggability 0.85

Structure

electron microscopy · 14 distinct chains · 25% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	DNA replication complex gins protein PSF1	protein	208	41% helix, 3% strand	Q12488
B	DNA replication complex gins protein PSF2	protein	186	29% helix, 4% strand	P40359
C	DNA replication complex gins protein PSF3	protein	159	31% helix, 10% strand	Q12146
D	DNA replication complex gins protein SLD5	protein	230	38% helix, 7% strand	Q03406
c	Cell division control protein 45	protein	553	37% helix, 10% strand	Q08032
2	DNA replication licensing factor MCM2 (EC 3.6.4.12)	protein	260	17% helix, 17% strand	P29469
3	DNA replication licensing factor MCM3 (EC 3.6.4.12)	protein	270	19% helix, 19% strand	P24279
4	DNA replication licensing factor MCM4 (EC 3.6.4.12)	protein	285	18% helix, 22% strand	P30665
5	Minichromosome maintenance protein 5 (EC 3.6.4.12)	protein	252	15% helix, 28% strand	P29496
6	DNA replication licensing factor MCM6 (EC 3.6.4.12)	protein	273	21% helix, 19% strand	P53091
7	DNA replication licensing factor MCM7 (EC 3.6.4.12)	protein	326	17% helix, 17% strand	P38132
E	DNA polymerase alpha-binding protein	protein	424	24% helix, 26% strand	Q01454
F	DNA polymerase alpha-binding protein	protein	431	24% helix, 26% strand	Q01454
G	DNA polymerase alpha-binding protein	protein	423	24% helix, 26% strand	Q01454

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1140	0.85	0.86	125	empty
2	826	0.83	0.85	91	empty
3	975	0.82	0.83	92	empty
4	1124	0.80	0.81	112	empty
5	947	0.79	0.81	96	empty

Interfaces

28 interfaces between chains.

B–D · 2288 Å² buried · 10 hydrogen bonds · protein-protein
A–D · 1951 Å² buried · 22 hydrogen bonds · protein-protein
3–7 · 1744 Å² buried · 13 hydrogen bonds · protein-protein
4–7 · 1573 Å² buried · 14 hydrogen bonds · protein-protein
4–6 · 1498 Å² buried · 9 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

6PTJ · Structure of Ctf4 trimer in complex with one CMG helicase · the same entry in another collection · chain 5 against 5, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q12488
Every structure of UniProt P40359
Every structure of UniProt Q12146
Every structure of UniProt Q03406
Every structure of UniProt Q08032
Every structure of UniProt P29469
Every structure of UniProt P24279
Every structure of UniProt P30665
Every structure of UniProt P29496
Every structure of UniProt P53091
Every structure of UniProt P38132
Every structure of UniProt Q01454
Elsewhere: RCSB PDB 6PTJ · PDBe 6PTJ · UniProt Q12488 · UniProt P40359 · UniProt Q12146 · UniProt Q03406 · UniProt Q08032 · UniProt P29469 · UniProt P24279 · UniProt P30665 · UniProt P29496 · UniProt P53091 · UniProt P38132 · UniProt Q01454

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