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Mono-zinc vim-26. LEU224 in vim-26 from klebsiella pneumoniae has implications for drug binding.

Analyse Mono-zinc vim-26. LEU224 in vim-26 from klebsiella pneumoniae has implications… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4UWR
Type: protein
Length: 230 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Metallo-beta-lactamase vim-26
UniProt: E5BDC6
Ligands: NA, ZN
Pockets: 1 · best druggability 0.48

Structure

x-ray diffraction · 1 distinct chain · 27% helix, 28% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B	Metallo-beta-lactamase vim-26	protein	230	27% helix, 28% strand	E5BDC6

Ligands and binding sites

NA · Sodium ion · metal · 2 copies · chains B
ZN · Zinc ion · metal · chains B
FMT · Formic acid · additive · chains 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	134	0.48	0.78	20	empty

Modifications

Observed in the structure: 1 modified (oxidation).

Compared structures

4UWR · Mono-zinc VIM-26. Leu224 in VIM-26 from Klebsiella pneumoniae has implications for drug… · the same entry in another collection · chain B against B, 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 E5BDC6
Elsewhere: RCSB PDB 4UWR · PDBe 4UWR · UniProt E5BDC6

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