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Crystal structure of yeast DNA polymerase alpha, selenomethionine protein

Analyse Crystal structure of yeast DNA polymerase alpha, selenomethionine protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4B08
Type: protein
Length: 827 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: DNA polymerase alpha catalytic subunit a
EC: 2.7.7.7
UniProt: P13382
Pockets: 13 · best druggability 0.67

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	DNA polymerase alpha catalytic subunit a (EC 2.7.7.7)	protein	827	39% helix, 22% strand	P13382

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	668	0.67	0.76	61	empty
2	129	0.65	0.88	22	empty
3	378	0.64	0.79	43	empty
4	551	0.64	0.76	59	empty
5	157	0.63	0.85	23	empty

Modifications

Observed in the structure: 28 modified (engineered).

Compared structures

4B08 · Yeast DNA polymerase alpha, Selenomethionine protein · the same entry in another collection · chain A against A, TM-score 1.00
P13382 · AlphaFold monomer V2.0 prediction for DNA polymerase alpha catalytic subunit a (P13382) · a predicted model of the same protein · chain A against A, TM-score 0.87

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 P13382
Elsewhere: RCSB PDB 4B08 · PDBe 4B08 · UniProt P13382

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