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Crystal structure of APE1195

Analyse Crystal structure of APE1195 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2YVU
Type: protein
Length: 351 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Probable adenylyl-sulfate kinase
EC: 2.7.1.25
UniProt: Q9YCR6
Pockets: 2 · best druggability 0.64

Structure

x-ray diffraction · 2 distinct chains · 49% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Probable adenylyl-sulfate kinase (EC 2.7.1.25)	protein	179	48% helix, 15% strand	Q9YCR6
B	Probable adenylyl-sulfate kinase (EC 2.7.1.25)	protein	172	49% helix, 16% strand	Q9YCR6

Pockets

2 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	519	0.64	0.76	53	empty
2	336	0.64	0.79	35	empty

Interfaces

1 interface between chains.

A–B · 1146 Å² buried · 22 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

2YVU · Crystal structure of APE1195 · the same entry in another collection · chain A against A, TM-score 1.00
Q9YCR6 · AlphaFold monomer V2.0 prediction for probable adenylyl-sulfate kinase (Q9YCR6) · a predicted model of the same protein · chain B 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 Q9YCR6
Elsewhere: RCSB PDB 2YVU · PDBe 2YVU · UniProt Q9YCR6

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