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Crystal structure of a putative metal-dependent hydrolase (AVA_3068) from anabaena variabilis atcc 29413 at 1.65 a resolution

Analyse Crystal structure of a putative metal-dependent hydrolase (AVA_3068) from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2P97
Type: protein
Length: 402 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Hypothetical protein
UniProt: Q3M8K9
Ligands: MG, CL
Pockets: 1 · best druggability 0.78

Structure

x-ray diffraction · 1 distinct chain · 24% helix, 30% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Hypothetical protein	protein	201	24% helix, 30% strand	Q3M8K9

Ligands and binding sites

MG · Magnesium ion · metal · 2 copies · chains A, B
CL · Chloride ion · ion · chains B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	325	0.78	0.89	50	empty

Interfaces

1 interface between chains.

A–B · 1093 Å² buried · 19 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 modified (engineered).

Compared structures

2P97 · Crystal structure of a putative metal-dependent hydrolase (AVA_3068) from anabaena… · 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 Q3M8K9
Elsewhere: RCSB PDB 2P97 · PDBe 2P97 · UniProt Q3M8K9

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