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Crystal structure of TRIAP1-mbp fusion

Analyse Crystal structure of TRIAP1-mbp fusion in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4XZS
Type: protein
Length: 841 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Maltose-binding periplasmic PROTEIN,TP53-regulated inhibitor of apoptosis 1
UniProt: P0AEX9, O43715
Ligands: GLC
Pockets: 6 · best druggability 0.78

Structure

x-ray diffraction · 2 distinct chains · 50% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Maltose-binding periplasmic PROTEIN,TP53-regulated inhibitor of apoptosis 1	protein	421	50% helix, 17% strand	P0AEX9, O43715
B	Maltose-binding periplasmic PROTEIN,TP53-regulated inhibitor of apoptosis 1	protein	420	50% helix, 18% strand	P0AEX9, O43715

Ligands and binding sites

GLC · alpha-D-glucopyranose · sugar · 4 copies · chains A, B

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

Pockets

6 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	615	0.78	0.84	70	empty
2	347	0.77	0.88	39	GLC
3	261	0.68	0.84	29	GLC
4	289	0.53	0.75	39	empty
5	88	0.44	0.80	20	empty

Interfaces

1 interface between chains.

A–B · 488 Å² buried · 4 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

4XZS · Crystal Structure of TRIAP1-MBP fusion · the same entry in another collection · chain A against A, TM-score 1.00
O43715 · AlphaFold monomer V2.0 prediction for TP53-regulated inhibitor of apoptosis 1 (O43715) · a predicted model of the same protein · chain A against A, TM-score 0.11

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 P0AEX9
Every structure of UniProt O43715
Elsewhere: RCSB PDB 4XZS · PDBe 4XZS · UniProt P0AEX9 · UniProt O43715

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