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DNA polymerase sliding clamp from escherichia COLI with peptide 37 bound

Analyse DNA polymerase sliding clamp from escherichia COLI with peptide 37 bound in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7AZ7
Type: protein
Length: 372 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Beta sliding clamp; Peptide 37
UniProt: A0A073FMV0
Pockets: 2 · best druggability 0.44

Structure

x-ray diffraction · 2 distinct chains · 22% helix, 44% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Beta sliding clamp	protein	366	23% helix, 45% strand	A0A073FMV0
H	Peptide 37	protein	6	0% helix, 17% strand	—

Ligands and binding sites

FMT · Formic acid · additive · chains A
1PE · Pentaethylene glycol · additive · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

2 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	90	0.44	0.79	15	empty
2	51	0.29	0.75	17	1PE

Interfaces

1 interface between chains.

A–H · 675 Å² buried · 8 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 modified (nonstandard).

Compared structures

7AZ7 · DNA polymerase sliding clamp from Escherichia coli with peptide 37 bound · 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 A0A073FMV0
Elsewhere: RCSB PDB 7AZ7 · PDBe 7AZ7 · UniProt A0A073FMV0

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