Research workbench

Crystal structure of REV7-WT/REV3 as a monomer under high-salt conditions

Analyse Crystal structure of REV7-WT/REV3 as a monomer under high-salt conditions in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6BI7
Type: protein
Length: 788 residues
Chains: 8
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Mitotic spindle assembly checkpoint protein MAD2B; DNA polymerase zeta catalytic subunit
EC: 2.7.7.7
UniProt: Q9UI95, O60673
Pockets: 6 · best druggability 0.70

Structure

x-ray diffraction · 8 distinct chains · 38% helix, 28% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Mitotic spindle assembly checkpoint protein MAD2B	protein	186	36% helix, 32% strand	Q9UI95
B	DNA polymerase zeta catalytic subunit (EC 2.7.7.7)	protein	23	39% helix, 26% strand	O60673
C	Mitotic spindle assembly checkpoint protein MAD2B	protein	182	38% helix, 31% strand	Q9UI95
D	DNA polymerase zeta catalytic subunit (EC 2.7.7.7)	protein	26	35% helix, 19% strand	O60673
E	Mitotic spindle assembly checkpoint protein MAD2B	protein	174	38% helix, 26% strand	Q9UI95
F	DNA polymerase zeta catalytic subunit (EC 2.7.7.7)	protein	21	43% helix, 14% strand	O60673
G	Mitotic spindle assembly checkpoint protein MAD2B	protein	154	40% helix, 29% strand	Q9UI95
H	DNA polymerase zeta catalytic subunit (EC 2.7.7.7)	protein	22	41% helix, 14% strand	O60673

Pockets

6 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	800	0.70	0.76	55	empty
2	615	0.65	0.76	48	empty
3	483	0.62	0.75	60	empty
4	233	0.50	0.75	40	empty
5	59	0.31	0.76	13	empty

Interfaces

13 interfaces between chains.

C–D · 1382 Å² buried · 18 hydrogen bonds · protein-protein
A–B · 1353 Å² buried · 15 hydrogen bonds · protein-protein
E–F · 1142 Å² buried · 13 hydrogen bonds · protein-protein
G–H · 1108 Å² buried · 12 hydrogen bonds · protein-protein
A–C · 580 Å² buried · 10 hydrogen bonds · protein-protein

Compared structures

6BI7 · Crystal structure of Rev7-WT/Rev3 as a monomer under high-salt conditions · the same entry in another collection · chain H against H, TM-score 1.00
Q9UI95 · AlphaFold monomer V2.0 prediction for mitotic spindle assembly checkpoint protein MAD2B… · a predicted model of the same protein · chain G against A, TM-score 0.98

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 Q9UI95
Every structure of UniProt O60673
Elsewhere: RCSB PDB 6BI7 · PDBe 6BI7 · UniProt Q9UI95 · UniProt O60673

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