MolNFT v1 · #77793 · protein

Structure of the full-length major pilin rrgb from streptococcus pneumoniae

3RPK · Backbone pilus subunit: “Structure of the full-length major pilin rrgb from streptococcus pneumoniae”. X-ray diffraction, 18 pockets (best druggability 0.74). MolNFT v1 #77793 on GenesisL1: 3D structure, binding sites and pockets in…

PDB: 3RPK
Type: protein
Length: 1,180 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Backbone pilus subunit
UniProt: A7KT39
Pockets: 18 · best druggability 0.74

Structure

x-ray diffraction · 1 distinct chain · 10% helix, 39% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Backbone pilus subunit	protein	590	10% helix, 39% strand	A7KT39

Pockets

18 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	664	0.74	0.80	60	empty
2	478	0.73	0.82	63	empty
3	336	0.69	0.83	44	empty
4	177	0.55	0.80	46	empty
5	100	0.55	0.85	24	empty

Interfaces

1 interface between chains.

A–B · 2226 Å² buried · 26 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 10 modified, 6 isopeptide (engineered, isopeptide).

Compared structures

3RPK · Structure of the Full-Length Major Pilin RrgB from Streptococcus pneumoniae · the same entry in another collection · chain B against B, 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 A7KT39
Elsewhere: RCSB PDB 3RPK · PDBe 3RPK · UniProt A7KT39

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