MolNFT v1 · #156066 · protein

Ribonuclease from hericium erinaceus active and gmp binding form

6LS1 · Ribonuclease T1: “Ribonuclease from hericium erinaceus active and gmp binding form”. X-ray diffraction, 2 ligands (GMP, SO4), 1 pocket (best druggability 0.28). MolNFT v1 #156066 on GenesisL1: 3D structure, binding sites and pockets…

PDB: 6LS1
Type: protein
Length: 200 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ribonuclease T1
UniProt: B1Q4V2
Ligands: GMP, SO4
Pockets: 1 · best druggability 0.28

Structure

x-ray diffraction · 1 distinct chain · 11% helix, 31% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Ribonuclease T1	protein	100	11% helix, 31% strand	B1Q4V2

Ligands and binding sites

GMP · Guanosine · ligand · chains A
SO4 · Sulfate ion · ion · chains B
PEG · Di(hydroxyethyl)ether · additive · chains A

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

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	69	0.28	0.73	21	empty

Interfaces

1 interface between chains.

A–B · 367 Å² buried · 5 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 disulfide (disulfide).

Compared structures

6LS1 · Ribonuclease from Hericium erinaceus active and GMP binding form · 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 B1Q4V2
Elsewhere: RCSB PDB 6LS1 · PDBe 6LS1 · UniProt B1Q4V2

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