MolNFT v1 · #98473 · protein

Crystal structure of cordyceps militaris idcase D323N mutant in apo form

4LAK · Uracil-5-carboxylate decarboxylase: “Crystal structure of cordyceps militaris idcase D323N mutant in apo form”. X-ray diffraction, 1 ligand (ZN), 12 pockets (best druggability 0.77). MolNFT v1 #98473 on GenesisL1: 3D structure…

PDB: 4LAK
Type: protein
Length: 698 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Uracil-5-carboxylate decarboxylase
UniProt: G3J531
Ligands: ZN
Pockets: 12 · best druggability 0.77

Structure

x-ray diffraction · 2 distinct chains · 50% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Uracil-5-carboxylate decarboxylase	protein	336	50% helix, 12% strand	G3J531
B	Uracil-5-carboxylate decarboxylase	protein	362	50% helix, 14% strand	G3J531

Ligands and binding sites

ZN · Zinc ion · metal · 2 copies · chains A, B

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

Pockets

12 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	357	0.77	0.87	51	empty
2	561	0.69	0.78	47	empty
3	197	0.51	0.77	29	empty
4	115	0.50	0.80	19	empty
5	100	0.44	0.79	15	empty

Interfaces

1 interface between chains.

A–B · 2836 Å² buried · 16 hydrogen bonds · protein-protein

Compared structures

4LAK · Crystal structure of Cordyceps militaris IDCase D323N mutant in apo 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 G3J531
Elsewhere: RCSB PDB 4LAK · PDBe 4LAK · UniProt G3J531

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