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Kod-ri incorporating DNA, N+2

Analyse Kod-ri incorporating DNA, N+2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7RSS
Type: protein + DNA
Length: 784 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: DNA polymerase; Template; Primer
EC: 2.7.7.7
UniProt: D0VWU9
Pockets: 7 · best druggability 0.80

Structure

x-ray diffraction · 3 distinct chains · 42% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	DNA polymerase (EC 2.7.7.7)	protein	756	42% helix, 23% strand	D0VWU9
T	Template	dna	15	—	—
P	Primer	dna	13	—	—

Pockets

7 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	1155	0.80	0.81	102	empty
2	232	0.78	0.92	36	empty
3	323	0.68	0.82	56	empty
4	260	0.54	0.76	32	empty
5	82	0.39	0.77	17	empty

Interfaces

3 interfaces between chains.

A–T · 1107 Å² buried · 20 hydrogen bonds · protein-nucleic
A–P · 761 Å² buried · 24 hydrogen bonds · protein-nucleic
T–P · 617 Å² buried · 64 hydrogen bonds · nucleic-nucleic

Compared structures

7RSS · Kod-RI incorporating DNA, n+2 · the same entry in another collection · chain A against A, 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 D0VWU9
Elsewhere: RCSB PDB 7RSS · PDBe 7RSS · UniProt D0VWU9

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