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Crystal structure of mazf (form-II) from deinococcus radiodurans

Analyse Crystal structure of mazf (form-II) from deinococcus radiodurans in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7D2M
Type: protein
Length: 223 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Endoribonuclease mazf
EC: 3.1.27.-
UniProt: A0A6G9BVQ8
Ligands: 3PO, SO4
Pockets: 1 · best druggability 0.37

Structure

x-ray diffraction · 2 distinct chains · 25% helix, 31% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B	Endoribonuclease mazf (EC 3.1.27.-)	protein	112	24% helix, 31% strand	A0A6G9BVQ8
C	Endoribonuclease mazf (EC 3.1.27.-)	protein	111	25% helix, 32% strand	A0A6G9BVQ8

Ligands and binding sites

3PO · Triphosphate · ligand · chains B
SO4 · Sulfate ion · ion · 2 copies · chains B, C

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

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	98	0.37	0.75	15	empty

Interfaces

1 interface between chains.

B–C · 1309 Å² buried · 24 hydrogen bonds · protein-protein

Compared structures

7D2M · Crystal structure of MazF (Form-II) from Deinococcus radiodurans · the same entry in another collection · chain B against B, 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 A0A6G9BVQ8
Elsewhere: RCSB PDB 7D2M · PDBe 7D2M · UniProt A0A6G9BVQ8

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