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Crystal structure of PIF1 helicase from bacteroides double mutant L95C-I339C

Analyse Crystal structure of PIF1 helicase from bacteroides double mutant L95C-I339C in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5FTF
Type: protein
Length: 431 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Tpr domain protein
EC: 3.6.4.12
UniProt: D7K0H3
Ligands: ADP
Pockets: 5 · best druggability 0.80

Structure

x-ray diffraction · 1 distinct chain · 32% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Tpr domain protein (EC 3.6.4.12)	protein	431	32% helix, 25% strand	D7K0H3

Ligands and binding sites

ADP · Adenosine-5'-diphosphate · ligand · chains A

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

Pockets

5 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	1100	0.80	0.81	108	ADP
2	228	0.57	0.79	33	empty
3	51	0.37	0.80	17	empty
4	50	0.33	0.78	18	empty
5	54	0.32	0.77	16	empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

5FTF · Crystal structure of Pif1 helicase from Bacteroides double mutant L95C-I339C · 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 D7K0H3
Elsewhere: RCSB PDB 5FTF · PDBe 5FTF · UniProt D7K0H3

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