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Crystal structure of PA1268 solved by sulfur sad

Analyse Crystal structure of PA1268 solved by sulfur sad in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2AZP
Type: protein
Length: 318 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Hypothetical protein PA1268
UniProt: Q9I476
Pockets: 2 · best druggability 0.37

Structure

x-ray diffraction · 1 distinct chain · 20% helix, 38% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Hypothetical protein PA1268	protein	318	20% helix, 38% strand	Q9I476

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	98	0.37	0.75	22	empty
2	52	0.25	0.73	13	empty

Compared structures

2AZP · Crystal Structure of PA1268 Solved by Sulfur SAD · the same entry in another collection · chain A against A, TM-score 1.00
Q9I476 · AlphaFold monomer V2.0 prediction for 4-hydroxyproline 2-epimerase (Q9I476) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 Q9I476
Elsewhere: RCSB PDB 2AZP · PDBe 2AZP · UniProt Q9I476

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