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Crystal structure of AFC3PO

Analyse Crystal structure of AFC3PO in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3ZC1
Type: protein
Length: 1,512 residues
Chains: 8
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Aftrax
UniProt: O28024
Ligands: MG
Pockets: 20 · best druggability 0.77

Structure

x-ray diffraction · 3 distinct chains · 78% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, E, F	Aftrax	protein	190	75% helix, 0% strand	O28024
C, G	Aftrax	protein	189	80% helix, 0% strand	O28024
D, H	Aftrax	protein	187	80% helix, 0% strand	O28024

Ligands and binding sites

MG · Magnesium ion · metal · 5 copies · chains B, C, D, F, G

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	1004	0.77	0.79	95	MG
2	1185	0.77	0.79	128	MG
3	1063	0.73	0.76	92	empty
4	488	0.67	0.78	52	empty
5	422	0.67	0.79	51	empty

Interfaces

20 interfaces between chains.

D–G · 1596 Å² buried · 9 hydrogen bonds · protein-protein
C–H · 1570 Å² buried · 8 hydrogen bonds · protein-protein
B–E · 1537 Å² buried · 9 hydrogen bonds · protein-protein
A–F · 1506 Å² buried · 4 hydrogen bonds · protein-protein
E–F · 823 Å² buried · 9 hydrogen bonds · protein-protein

Compared structures

3ZC1 · Crystal structure of AfC3PO · 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 O28024
Elsewhere: RCSB PDB 3ZC1 · PDBe 3ZC1 · UniProt O28024

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