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P4 protein from bacteriophage PHI12 in complex with ADP

Analyse P4 protein from bacteriophage PHI12 in complex with ADP in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1W44
Type: protein
Length: 912 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: NTPase P4
UniProt: Q94M05
Ligands: ADP
Pockets: 8 · best druggability 0.82

Structure

x-ray diffraction · 1 distinct chain · 32% helix, 31% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C	NTPase P4	protein	304	32% helix, 31% strand	Q94M05

Ligands and binding sites

ADP · Adenosine-5'-diphosphate · ligand · 3 copies · chains A, B, C

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

Pockets

8 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	968	0.82	0.83	106	ADP
2	663	0.78	0.83	65	empty
3	720	0.77	0.82	69	empty
4	248	0.73	0.88	34	ADP
5	376	0.57	0.75	47	empty

Interfaces

2 interfaces between chains.

B–C · 1972 Å² buried · 26 hydrogen bonds · protein-protein
A–B · 1942 Å² buried · 28 hydrogen bonds · protein-protein

Compared structures

1W44 · P4 protein from Bacteriophage PHI12 in complex with ADP · 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 Q94M05
Elsewhere: RCSB PDB 1W44 · PDBe 1W44 · UniProt Q94M05

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