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Crystal structure of fused zn-dependent AMIDASE/PEPTIDASE/PEPTODOGLYCAN-binding domain-containing protein from clostridium acetobutylicum atcc 824

Analyse Crystal structure of fused zn-dependent AMIDASE/PEPTIDASE/PEPTODOGLYCAN-binding… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4XXT
Type: protein
Length: 221 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Fusion of predicted zn-dependent AMIDASE/PEPTIDASE (cell wall…
UniProt: Q97I32
Pockets: 1 · best druggability 0.40

Structure

x-ray diffraction · 1 distinct chain · 29% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Fusion of predicted zn-dependent AMIDASE/PEPTIDASE (cell wall HYDROLASE/DD-carboxypeptidase family) and uncharacterized domain of erfk family peptodoglycan-binding domain	protein	221	29% helix, 26% strand	Q97I32

Ligands and binding sites

EDO · 1,2-ethanediol · additive · 3 copies · chains A
IMD · Imidazole · additive · 2 copies · chains A
ACT · Acetate ion · additive · 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	69	0.40	0.79	16	ACT

Modifications

Observed in the structure: 3 modified (engineered).

Compared structures

4XXT · Crystal structure of Fused Zn-dependent amidase/peptidase/peptodoglycan-binding… · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

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Every structure of UniProt Q97I32
Elsewhere: RCSB PDB 4XXT · PDBe 4XXT · UniProt Q97I32

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