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Crystal structure of human C3PO complex

Analyse Crystal structure of human C3PO complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3PJA
Type: protein
Length: 2,585 residues
Chains: 12
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Translin; Translin-associated protein X
UniProt: Q15631, Q99598
Pockets: 20 · best druggability 0.80

Structure

x-ray diffraction · 11 distinct chains · 76% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, D	Translin	protein	212	77% helix, 0% strand	Q15631
B	Translin	protein	217	72% helix, 0% strand	Q15631
C	Translin	protein	214	76% helix, 0% strand	Q15631
E	Translin	protein	215	76% helix, 1% strand	Q15631
F	Translin	protein	213	77% helix, 0% strand	Q15631
G	Translin	protein	212	78% helix, 0% strand	Q15631
H	Translin	protein	216	72% helix, 0% strand	Q15631
I	Translin	protein	210	78% helix, 0% strand	Q15631
J	Translin-associated protein X	protein	219	79% helix, 0% strand	Q99598
K	Translin-associated protein X	protein	222	78% helix, 2% strand	Q99598
L	Translin-associated protein X	protein	223	78% helix, 2% strand	Q99598

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1140	0.80	0.81	84	empty
2	919	0.78	0.80	69	empty
3	921	0.78	0.80	82	empty
4	547	0.75	0.82	40	empty
5	697	0.75	0.80	45	empty

Interfaces

29 interfaces between chains.

A–E · 1839 Å² buried · 8 hydrogen bonds · protein-protein
B–D · 1811 Å² buried · 8 hydrogen bonds · protein-protein
C–L · 1769 Å² buried · 9 hydrogen bonds · protein-protein
F–K · 1754 Å² buried · 11 hydrogen bonds · protein-protein
F–L · 1299 Å² buried · 15 hydrogen bonds · protein-protein

Compared structures

3PJA · Crystal structure of human C3PO complex · the same entry in another collection · chain L against L, 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 Q15631
Every structure of UniProt Q99598
Elsewhere: RCSB PDB 3PJA · PDBe 3PJA · UniProt Q15631 · UniProt Q99598

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