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Sliding clamp, DNA polymerase

Analyse Sliding clamp, DNA polymerase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1B8H
Type: protein
Length: 695 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: DNA polymerase processivity component; DNA polymerase fragment
UniProt: O80164, Q38087
Pockets: 6 · best druggability 0.39

Structure

x-ray diffraction · 2 distinct chains · 18% helix, 38% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C	DNA polymerase processivity component	protein	228	18% helix, 40% strand	O80164
D	DNA polymerase fragment	protein	11	27% helix, 0% strand	Q38087

Pockets

6 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	69	0.39	0.79	18	empty
2	79	0.35	0.75	16	empty
3	81	0.33	0.74	19	empty
4	50	0.30	0.77	18	empty
5	58	0.27	0.74	11	empty

Interfaces

4 interfaces between chains.

B–D · 647 Å² buried · 4 hydrogen bonds · protein-protein
A–B · 495 Å² buried · 9 hydrogen bonds · protein-protein
A–C · 486 Å² buried · 8 hydrogen bonds · protein-protein
B–C · 475 Å² buried · 11 hydrogen bonds · protein-protein

Compared structures

1B8H · Sliding clamp, DNA polymerase · the same entry in another collection · chain C against C, 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 O80164
Every structure of UniProt Q38087
Elsewhere: RCSB PDB 1B8H · PDBe 1B8H · UniProt O80164 · UniProt Q38087

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