MolNFT v2 · #151423 · protein

Siderophore hydrolase EstB from Aspergillus fumigatus

6GUP: “Siderophore hydrolase EstB from Aspergillus fumigatus”. X-ray diffraction at 1.85. MolNFT v2 #151423 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6GUP
Type: protein
Length: 661 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.85
Source: Aspergillus fumigatus
UniProt: Q4WF56

Structure

x-ray diffraction · resolution 1.85 · 2 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	340	—	Q4WF56
B	—	protein	321	—	Q4WF56

Ligands and binding sites

GOL · Glycerol · additive · chains B

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

Compared structures

6GUP · Siderophore hydrolase estb from aspergillus fumigatus · the same entry in another collection · chain A against A, TM-score 1.00
Q4WF56 · AlphaFold monomer V2.0 prediction for fusarinine C esterase sidj (Q4WF56) · a predicted model of the same protein · chain B against A, TM-score 0.92

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 Q4WF56
Elsewhere: RCSB PDB 6GUP · PDBe 6GUP · UniProt Q4WF56

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