MolNFT v1 · #98975 · protein

Crystal structure of the L,D-transpeptidase (residues 123-326) from xylanimonas cellulosilytica dsm 15894

4LPQ · ERFK/YBIS/YCFS/YNHG family protein: “Crystal structure of the L,D-transpeptidase (residues 123-326) from xylanimonas cellulosilytica dsm 15894”. X-ray diffraction, 1 ligand (CL), 1 pocket (best druggability 0.41). MolNFT v1 #98975…

PDB: 4LPQ
Type: protein
Length: 204 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: ERFK/YBIS/YCFS/YNHG family protein
UniProt: D1BWR1
Ligands: CL
Pockets: 1 · best druggability 0.41

Structure

x-ray diffraction · 1 distinct chain · 23% helix, 30% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	ERFK/YBIS/YCFS/YNHG family protein	protein	204	23% helix, 30% strand	D1BWR1

Ligands and binding sites

CL · Chloride ion · ion · 4 copies · chains A

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	55	0.41	0.82	22	CL

Modifications

Observed in the structure: 6 modified (engineered).

Compared structures

4LPQ · Crystal structure of the L,D-transpeptidase (residues 123-326) from Xylanimonas… · 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 D1BWR1
Elsewhere: RCSB PDB 4LPQ · PDBe 4LPQ · UniProt D1BWR1

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