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Crystal structure of the catalytic core of human DNA polymerase kappa

Analyse Crystal structure of the catalytic core of human DNA polymerase kappa in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1T94
Type: protein
Length: 791 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Polymerase (DNA directed) kappa
UniProt: Q9UBT6
Pockets: 8 · best druggability 0.69

Structure

x-ray diffraction · 2 distinct chains · 43% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Polymerase (DNA directed) kappa	protein	409	42% helix, 17% strand	Q9UBT6
B	Polymerase (DNA directed) kappa	protein	382	44% helix, 20% strand	Q9UBT6

Pockets

8 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	521	0.69	0.79	46	empty
2	484	0.62	0.76	51	empty
3	193	0.47	0.75	25	empty
4	152	0.46	0.77	27	empty
5	75	0.38	0.78	16	empty

Interfaces

1 interface between chains.

A–B · 47 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

1T94 · Crystal structure of the catalytic core of human DNA polymerase kappa · the same entry in another collection · chain A against A, TM-score 1.00
Q9UBT6 · AlphaFold monomer V2.0 prediction for DNA polymerase kappa (Q9UBT6) · a predicted model of the same protein · chain A against A, TM-score 0.75

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 Q9UBT6
Elsewhere: RCSB PDB 1T94 · PDBe 1T94 · UniProt Q9UBT6

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