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Human ERP44 zinc-bound form

Analyse Human ERP44 zinc-bound form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5XWM
Type: protein
Length: 1,416 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Endoplasmic reticulum resident protein 44
UniProt: Q9BS26
Ligands: ZN, CL
Pockets: 19 · best druggability 0.83

Structure

x-ray diffraction · 4 distinct chains · 38% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Endoplasmic reticulum resident protein 44	protein	346	38% helix, 20% strand	Q9BS26
B	Endoplasmic reticulum resident protein 44	protein	354	38% helix, 19% strand	Q9BS26
C	Endoplasmic reticulum resident protein 44	protein	348	39% helix, 20% strand	Q9BS26
D	Endoplasmic reticulum resident protein 44	protein	368	36% helix, 19% strand	Q9BS26

Ligands and binding sites

ZN · Zinc ion · metal · 10 copies · chains A, C, B, D
CL · Chloride ion · ion · 8 copies · chains A, C, B, D

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

Pockets

19 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	930	0.83	0.85	80	ZN
2	840	0.78	0.82	75	empty
3	707	0.76	0.81	86	ZN, CL
4	216	0.71	0.87	34	empty
5	276	0.68	0.84	39	empty

Interfaces

3 interfaces between chains.

B–D · 2520 Å² buried · 30 hydrogen bonds · protein-protein
A–C · 1512 Å² buried · 19 hydrogen bonds · protein-protein
B–C · 1291 Å² buried · 14 hydrogen bonds · protein-protein

Compared structures

5XWM · human ERp44 zinc-bound form · the same entry in another collection · chain D against D, TM-score 1.00
Q9BS26 · AlphaFold monomer V2.0 prediction for endoplasmic reticulum resident protein 44 (Q9BS26) · a predicted model of the same protein · chain A against A, TM-score 0.70

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 Q9BS26
Elsewhere: RCSB PDB 5XWM · PDBe 5XWM · UniProt Q9BS26

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