MolNFT v1 · #180969 · protein

Asymmetric unit for phage qbeta T=4 particle

7LGE · Capsid protein: “Asymmetric unit for phage qbeta T=4 particle”. Electron microscopy, 5 pockets (best druggability 0.76). MolNFT v1 #180969 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 7LGE
Type: protein
Length: 528 residues
Chains: 4
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Capsid protein
UniProt: P03615
Pockets: 5 · best druggability 0.76

Structure

electron microscopy · 1 distinct chain · 19% helix, 44% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	Capsid protein	protein	132	19% helix, 44% strand	P03615

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	1086	0.76	0.78	89	empty
2	95	0.56	0.86	25	empty
3	197	0.47	0.75	34	empty
4	53	0.32	0.76	19	empty
5	55	0.31	0.77	15	empty

Interfaces

6 interfaces between chains.

C–D · 3440 Å² buried · 50 hydrogen bonds · protein-protein
A–B · 462 Å² buried · 5 hydrogen bonds · protein-protein
B–C · 447 Å² buried · 6 hydrogen bonds · protein-protein
A–C · 392 Å² buried · 1 hydrogen bond · protein-protein
A–D · 378 Å² buried · 3 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

7LGE · Asymmetric unit for phage Qbeta T=4 particle · 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 P03615
Elsewhere: RCSB PDB 7LGE · PDBe 7LGE · UniProt P03615

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