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Crystal structure of hemopexin fold protein CP4 from cow pea

Analyse Crystal structure of hemopexin fold protein CP4 from cow pea in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3OYO
Type: protein
Length: 450 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Hemopexin fold protein CP4
Ligands: CA, NA, CL
Pockets: 4 · best druggability 0.60

Structure

x-ray diffraction · 1 distinct chain · 14% helix, 42% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Hemopexin fold protein CP4	protein	225	14% helix, 42% strand	—

Ligands and binding sites

CA · Calcium ion · metal · 2 copies · chains A, B
NA · Sodium ion · metal · 2 copies · chains A, B
CL · Chloride ion · ion · 2 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, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	124	0.60	0.86	27	empty
2	104	0.59	0.86	26	empty
3	77	0.33	0.74	19	empty
4	53	0.32	0.77	15	empty

Interfaces

1 interface between chains.

A–B · 616 Å² buried · 12 hydrogen bonds · protein-protein

Compared structures

3OYO · Crystal structure of hemopexin fold protein CP4 from cow pea · 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
Elsewhere: RCSB PDB 3OYO · PDBe 3OYO

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