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Crystal structure of a putative heme oxygenase (ALR5027) from nostoc sp. pcc 7120 at 1.50 a resolution

Analyse Crystal structure of a putative heme oxygenase (ALR5027) from nostoc sp. pcc… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1VL7
Type: protein
Length: 270 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Hypothetical protein ALR5027
UniProt: Q8YMA7
Pockets: 4 · best druggability 0.56

Structure

x-ray diffraction · 1 distinct chain · 30% helix, 39% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Hypothetical protein ALR5027	protein	135	30% helix, 39% strand	Q8YMA7

Ligands and binding sites

EDO · 1,2-ethanediol · additive · 8 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, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	85	0.56	0.86	17	EDO
2	95	0.54	0.85	20	empty
3	86	0.53	0.84	18	EDO
4	94	0.49	0.82	24	empty

Interfaces

1 interface between chains.

A–B · 1776 Å² buried · 27 hydrogen bonds · protein-protein

Compared structures

1VL7 · Crystal structure of a putative heme oxygenase (alr5027) from nostoc sp. pcc 7120 at 1.50… · 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 Q8YMA7
Elsewhere: RCSB PDB 1VL7 · PDBe 1VL7 · UniProt Q8YMA7

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