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Crystal structure of ribonuclease MC1 N71T mutant

Analyse Crystal structure of ribonuclease MC1 N71T mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1UCG
Type: protein
Length: 380 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ribonuclease mc
EC: 3.1.27.1
UniProt: P23540
Ligands: MN
Pockets: 2 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 38% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Ribonuclease mc (EC 3.1.27.1)	protein	190	38% helix, 23% strand	P23540

Ligands and binding sites

MN · Manganese (II) ion · metal · 4 copies · chains A, B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1005	0.76	0.78	78	MN
2	50	0.31	0.77	17	empty

Interfaces

1 interface between chains.

A–B · 418 Å² buried · 5 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 disulfide (disulfide).

Compared structures

1UCG · Crystal structure of Ribonuclease MC1 N71T mutant · the same entry in another collection · chain A against A, TM-score 1.00
P23540 · AlphaFold monomer V2.0 prediction for ribonuclease mc (P23540) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 P23540
Elsewhere: RCSB PDB 1UCG · PDBe 1UCG · UniProt P23540

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