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Crystal structure of a putative phosphatase (NMA1982) from neisseria meningitidis Z2491 at 1.41 a resolution

Analyse Crystal structure of a putative phosphatase (NMA1982) from neisseria… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2F46
Type: protein
Length: 284 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Hypothetical protein
Ligands: UNL, CL
Pockets: 4 · best druggability 0.40

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Hypothetical protein	protein	142	46% helix, 14% strand	—

Ligands and binding sites

UNL · Unknown ligand · ligand · chains B
CL · Chloride ion · ion · 2 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	120	0.40	0.75	20	empty
2	63	0.37	0.79	15	empty
3	56	0.37	0.80	15	empty
4	60	0.30	0.75	22	UNL

Interfaces

1 interface between chains.

A–B · 243 Å² buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 modified (engineered).

Compared structures

2F46 · Crystal structure of a putative phosphatase (nma1982) from neisseria meningitidis z2491… · 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
Elsewhere: RCSB PDB 2F46 · PDBe 2F46

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