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Crystal structures of self-capping papd chaperone homodimers

Analyse Crystal structures of self-capping papd chaperone homodimers in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1QPX
Type: protein
Length: 408 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Papd chaperone
UniProt: P15319
Pockets: 6 · best druggability 0.63

Structure

x-ray diffraction · 2 distinct chains · 9% helix, 50% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Papd chaperone	protein	206	8% helix, 51% strand	P15319
B	Papd chaperone	protein	202	9% helix, 49% strand	P15319

Pockets

6 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	537	0.63	0.75	56	empty
2	149	0.58	0.83	22	empty
3	57	0.46	0.84	15	empty
4	104	0.39	0.76	22	empty
5	68	0.30	0.74	14	empty

Interfaces

1 interface between chains.

A–B · 707 Å² buried · 9 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 3 disulfide (disulfide).

Compared structures

1QPX · Crystal structures of self-capping papd chaperone homodimers · the same entry in another collection · chain A against A, TM-score 1.00
P15319 · AlphaFold monomer V2.0 prediction for chaperone protein papd (P15319) · a predicted model of the same protein · chain A against A, TM-score 0.96

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 P15319
Elsewhere: RCSB PDB 1QPX · PDBe 1QPX · UniProt P15319

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