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Rat ceruloplasmin trigonal form

Analyse Rat ceruloplasmin trigonal form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5N4L
Type: protein
Length: 2,068 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ceruloplasmin
UniProt: G3V7K3
Ligands: CU, CA, NA
Pockets: 20 · best druggability 0.87

Structure

x-ray diffraction · 1 distinct chain · 11% helix, 36% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Ceruloplasmin	protein	1034	11% helix, 36% strand	G3V7K3

Ligands and binding sites

CU · Copper (II) ion · metal · 11 copies · chains A, B
CA · Calcium ion · metal · 2 copies · chains A, B
NA · Sodium ion · metal · 2 copies · chains A, B

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

Pockets

20 pockets found on a 1 Å grid, 12 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	659	0.87	0.91	55	empty
2	861	0.84	0.86	90	empty
3	880	0.71	0.76	97	empty
4	306	0.67	0.82	38	empty
5	294	0.62	0.80	38	empty

Interfaces

1 interface between chains.

A–B · 392 Å² buried · 7 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 10 disulfide (disulfide).

Compared structures

5N4L · Rat ceruloplasmin trigonal form · 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 G3V7K3
Elsewhere: RCSB PDB 5N4L · PDBe 5N4L · UniProt G3V7K3

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