MolNFT v1 · #127419 · protein

Complex between the leucine zipper (lz) and centrosomin-motif 2 (CM2) domains of drosophila melanogaster centrosomin (cnn) - L535E mutant form

5MW0: “Complex between the leucine zipper (lz) and centrosomin-motif 2 (CM2) domains of drosophila melanogaster…”. X-ray diffraction, 1 ligand (ZN), 1 pocket (best druggability 0.54). MolNFT v1 #127419 on GenesisL1: 3D structure, binding…

PDB: 5MW0
Type: protein
Length: 222 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Centrosomin
UniProt: P54623
Ligands: ZN
Pockets: 1 · best druggability 0.54

Structure

x-ray diffraction · 4 distinct chains · 90% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Centrosomin	protein	62	90% helix, 0% strand	P54623
C	Centrosomin	protein	49	86% helix, 0% strand	P54623
D	Centrosomin	protein	51	88% helix, 0% strand	P54623
B	Centrosomin	protein	60	93% helix, 0% strand	P54623

Ligands and binding sites

ZN · Zinc ion · metal · chains A, B

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

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	140	0.54	0.81	19	empty

Interfaces

6 interfaces between chains.

A–B · 962 Å² buried · 8 hydrogen bonds · protein-protein
C–D · 940 Å² buried · 1 hydrogen bond · protein-protein
A–D · 394 Å² buried · 0 hydrogen bonds · protein-protein
C–B · 392 Å² buried · 0 hydrogen bonds · protein-protein
A–C · 379 Å² buried · 5 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

5MW0 · Complex between the Leucine Zipper (LZ) and Centrosomin-motif 2 (CM2) domains of… · the same entry in another collection · chain B against B, TM-score 1.00
P54623 · AlphaFold monomer V2.0 prediction for centrosomin (P54623) · a predicted model of the same protein · chain D against A, TM-score 0.93

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 P54623
Elsewhere: RCSB PDB 5MW0 · PDBe 5MW0 · UniProt P54623

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