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Crystal structure of a had-like phosphatase from enterococcus faecalis V583

Analyse Crystal structure of a had-like phosphatase from enterococcus faecalis V583 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1YV9
Type: protein
Length: 514 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Hydrolase, haloacid dehalogenase family
UniProt: Q836C7
Ligands: PO4
Pockets: 4 · best druggability 0.80

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Hydrolase, haloacid dehalogenase family	protein	257	39% helix, 21% strand	Q836C7

Ligands and binding sites

PO4 · Phosphate ion · ion · 4 copies · chains A, B

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

Pockets

4 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	932	0.80	0.82	98	PO4
2	299	0.69	0.83	40	PO4
3	67	0.48	0.84	16	empty
4	94	0.46	0.80	23	empty

Interfaces

1 interface between chains.

A–B · 780 Å² buried · 7 hydrogen bonds · protein-protein

Compared structures

1YV9 · Crystal structure of a HAD-like phosphatase from Enterococcus faecalis V583 · 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 Q836C7
Elsewhere: RCSB PDB 1YV9 · PDBe 1YV9 · UniProt Q836C7

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