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Crystal structure of C-as lyase with mutation K105R with NI(II)

Analyse Crystal structure of C-as lyase with mutation K105R with NI(II) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6XA0
Type: protein
Length: 218 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: GLYOXALASE/BLEOMYCIN resistance PROTEIN/DIOXYGENASE
UniProt: D1A230
Ligands: NI
Pockets: 1 · best druggability 0.37

Structure

x-ray diffraction · 2 distinct chains · 23% helix, 43% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	GLYOXALASE/BLEOMYCIN resistance PROTEIN/DIOXYGENASE	protein	110	23% helix, 43% strand	D1A230
B	GLYOXALASE/BLEOMYCIN resistance PROTEIN/DIOXYGENASE	protein	108	23% helix, 43% strand	D1A230

Ligands and binding sites

NI · Nickel (II) ion · metal · 2 copies · 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	64	0.37	0.78	14	empty

Interfaces

1 interface between chains.

A–B · 1478 Å² buried · 19 hydrogen bonds · protein-protein

Compared structures

6XA0 · Crystal structure of C-As lyase with mutation K105R with Ni(II) · 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 D1A230
Elsewhere: RCSB PDB 6XA0 · PDBe 6XA0 · UniProt D1A230

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