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Crystal structure of cordyceps militaris idcase H195A mutant

Analyse Crystal structure of cordyceps militaris idcase H195A mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4LAN
Type: protein
Length: 739 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 0.70

Structure

x-ray diffraction · 2 distinct chains · 48% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Uracil-5-carboxylate decarboxylase	protein	370	47% helix, 13% strand	G3J531
B	Uracil-5-carboxylate decarboxylase	protein	369	48% helix, 13% 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, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	646	0.70	0.78	56	ZN
2	521	0.65	0.77	51	ZN
3	110	0.48	0.80	17	empty
4	105	0.45	0.79	18	empty
5	120	0.44	0.77	18	empty

Interfaces

1 interface between chains.

A–B · 2899 Å² buried · 15 hydrogen bonds · protein-protein

Compared structures

4LAN · Crystal structure of Cordyceps militaris IDCase H195A mutant · 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 4LAN · PDBe 4LAN · UniProt G3J531

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