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Crystal structure of PLIM_4148 protein from planctomyces limnophilus

Analyse Crystal structure of PLIM_4148 protein from planctomyces limnophilus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4H7L
Type: protein
Length: 232 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Uncharacterized protein
UniProt: D5SZ58
Ligands: CU
Pockets: 2 · best druggability 0.71

Structure

x-ray diffraction · 2 distinct chains · 3% helix, 49% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Uncharacterized protein	protein	115	3% helix, 50% strand	D5SZ58
B	Uncharacterized protein	protein	117	3% helix, 49% strand	D5SZ58

Ligands and binding sites

CU · Copper (II) ion · metal · 2 copies · chains A, B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	122	0.71	0.92	27	empty
2	147	0.67	0.88	26	empty

Interfaces

1 interface between chains.

A–B · 1407 Å² buried · 16 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 modified (engineered).

Compared structures

4H7L · Crystal structure of Plim_4148 protein from Planctomyces limnophilus · 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 D5SZ58
Elsewhere: RCSB PDB 4H7L · PDBe 4H7L · UniProt D5SZ58

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