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Crystal structure of MCPIP1 N-terminal conserved domain

Analyse Crystal structure of MCPIP1 N-terminal conserved domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3V32
Type: protein
Length: 312 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ribonuclease ZC3H12A
EC: 3.1.-.-
UniProt: Q5D1E8
Pockets: 1 · best druggability 0.66

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B, A	Ribonuclease ZC3H12A (EC 3.1.-.-)	protein	156	41% helix, 20% strand	Q5D1E8

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	515	0.66	0.77	38	empty

Interfaces

1 interface between chains.

B–A · 243 Å² buried · 6 hydrogen bonds · protein-protein

Compared structures

3V32 · Crystal structure of MCPIP1 N-terminal conserved domain · the same entry in another collection · chain B against B, TM-score 1.00
Q5D1E8 · AlphaFold monomer V2.0 prediction for endoribonuclease ZC3H12A (Q5D1E8) · a predicted model of the same protein · chain B against A, TM-score 0.98

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 Q5D1E8
Elsewhere: RCSB PDB 3V32 · PDBe 3V32 · UniProt Q5D1E8

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