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Structure of the catalytic domain of xlya

Analyse Structure of the catalytic domain of xlya in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3RDR
Type: protein
Length: 153 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: N-acetylmuramoyl-L-alanine amidase xlya
EC: 3.5.1.28
UniProt: P39800
Ligands: ZN, CL

Structure

x-ray diffraction · 1 distinct chain · 31% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	N-acetylmuramoyl-L-alanine amidase xlya (EC 3.5.1.28)	protein	153	31% helix, 17% strand	P39800

Ligands and binding sites

ZN · Zinc ion · metal · chains A
CL · Chloride ion · ion · chains A

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

Compared structures

3RDR · Structure of the catalytic domain of XlyA · the same entry in another collection · chain A against A, TM-score 1.00
P39800 · AlphaFold monomer V2.0 prediction for N-acetylmuramoyl-L-alanine amidase xlya (P39800) · a predicted model of the same protein · chain A against A, TM-score 0.99

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Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P39800
Elsewhere: RCSB PDB 3RDR · PDBe 3RDR · UniProt P39800

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