Research workbench

Type 1 copper-binding loop of nitrite reductase mutant: 130- capegmvpwhvvsgm-144 to 130-ctphpfm-136

Analyse Type 1 copper-binding loop of nitrite reductase mutant: 130… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2VMJ
Type: protein
Length: 326 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Dissimilatory copper-containing nitrite reductase
UniProt: O68601
Ligands: ZN
Pockets: 2 · best druggability 0.64

Structure

x-ray diffraction · 1 distinct chain · 9% helix, 42% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Dissimilatory copper-containing nitrite reductase	protein	326	9% helix, 42% strand	O68601

Ligands and binding sites

ZN · Zinc ion · metal · 3 copies · chains A
EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · additive · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	167	0.64	0.84	29	empty
2	76	0.36	0.77	16	empty

Compared structures

2VMJ · Type 1 Copper-Binding Loop of Nitrite Reductase mutant: 130- CAPEGMVPWHVVSGM-144 to… · 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 O68601
Elsewhere: RCSB PDB 2VMJ · PDBe 2VMJ · UniProt O68601

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