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Crystal structure of PIF1 helicase from bacteroides in complex with amppnp

Analyse Crystal structure of PIF1 helicase from bacteroides in complex with amppnp in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5FTB
Type: protein
Length: 429 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: ANP, K, MG
Pockets: 6 · best druggability 0.77

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	429	32% helix, 25% strand	D7K0H3

Ligands and binding sites

ANP · Phosphoaminophosphonic acid-adenylate ester · ligand · chains A
K · Potassium ion · metal · 9 copies · chains A
MG · Magnesium ion · metal · chains A

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

Pockets

6 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	1035	0.77	0.79	79	K, ANP, MG
2	277	0.56	0.76	36	empty
3	116	0.42	0.77	27	empty
4	66	0.31	0.74	15	empty
5	50	0.28	0.75	15	empty

Compared structures

5FTB · Crystal structure of Pif1 helicase from Bacteroides in complex with AMPPNP · 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 5FTB · PDBe 5FTB · UniProt D7K0H3

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