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X-ray structure of native peptide amidase from stenotrophomonas maltophilia at 1.4 a

Analyse X-ray structure of native peptide amidase from stenotrophomonas maltophilia at… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1M22
Type: protein
Length: 974 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Peptide amidase
EC: 3.5.1.-
UniProt: Q8RJN5
Pockets: 8 · best druggability 0.61

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Peptide amidase (EC 3.5.1.-)	protein	487	40% helix, 15% strand	Q8RJN5

Ligands and binding sites

EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · additive · 2 copies · chains A, B

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

Pockets

8 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	426	0.61	0.76	42	empty
2	86	0.61	0.89	29	empty
3	387	0.60	0.76	33	empty
4	148	0.54	0.81	38	EPE
5	77	0.42	0.80	19	empty

Interfaces

1 interface between chains.

A–B · 28 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

1M22 · X-ray structure of native peptide amidase from Stenotrophomonas maltophilia at 1.4 A · 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 Q8RJN5
Elsewhere: RCSB PDB 1M22 · PDBe 1M22 · UniProt Q8RJN5

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