MolNFT v1 · #81025 · protein

Crystal structure of human survivin K62A mutant

3UEG · Baculoviral iap repeat-containing protein 5: “Crystal structure of human survivin K62A mutant”. X-ray diffraction, 1 ligand (ZN), 2 pockets (best druggability 0.53). MolNFT v1 #81025 on GenesisL1: 3D structure, binding sites and…

PDB: 3UEG
Type: protein
Length: 275 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Baculoviral iap repeat-containing protein 5
UniProt: O15392
Ligands: ZN
Pockets: 2 · best druggability 0.53

Structure

x-ray diffraction · 2 distinct chains · 56% helix, 7% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Baculoviral iap repeat-containing protein 5	protein	137	56% helix, 7% strand	O15392
B	Baculoviral iap repeat-containing protein 5	protein	138	56% helix, 7% strand	O15392

Ligands and binding sites

ZN · Zinc ion · metal · 2 copies · chains A, B
EDO · 1,2-ethanediol · additive · chains A
PG4 · Tetraethylene glycol · additive · chains A

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

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	113	0.53	0.82	20	empty
2	119	0.53	0.81	20	empty

Interfaces

1 interface between chains.

A–B · 552 Å² buried · 6 hydrogen bonds · protein-protein

Compared structures

3UEG · Crystal structure of human Survivin K62A mutant · the same entry in another collection · chain A against A, TM-score 1.00
O15392 · AlphaFold monomer V2.0 prediction for baculoviral iap repeat- containing protein 5… · a predicted model of the same protein · chain B against A, TM-score 0.99

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 O15392
Elsewhere: RCSB PDB 3UEG · PDBe 3UEG · UniProt O15392

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