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Crystal structure of amidohydrolase PMI1525 (target efi-500319) from proteus mirabilis HI4320, a complex with butyric acid and manganese

Analyse Crystal structure of amidohydrolase PMI1525 (target efi-500319) from proteus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4QSF
Type: protein
Length: 354 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Amidohydrolase PMI1525
UniProt: B4EXV8
Ligands: BUA, MN, SO4
Pockets: 2 · best druggability 0.75

Structure

x-ray diffraction · 1 distinct chain · 46% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Amidohydrolase PMI1525	protein	354	46% helix, 14% strand	B4EXV8

Ligands and binding sites

BUA · butanoic acid · ligand · chains A
MN · Manganese (II) ion · metal · 2 copies · chains A
SO4 · Sulfate ion · ion · 2 copies · chains A

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

Pockets

2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	283	0.75	0.88	35	BUA
2	62	0.50	0.86	16	empty

Compared structures

4QSF · CRYSTAL STRUCTURE of AMIDOHYDROLASE PMI1525 (TARGET EFI-500319) FROM PROTEUS MIRABILIS… · the same entry in another collection · chain A against A, TM-score 1.00

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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 B4EXV8
Elsewhere: RCSB PDB 4QSF · PDBe 4QSF · UniProt B4EXV8

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