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4BJU

Genetic and structural validation of Aspergillus fumigatus N- acetylphosphoglucosamine mutase as an antifungal target

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0004610molecular_functionphosphoacetylglucosamine mutase activity
A0005975biological_processcarbohydrate metabolic process
A0006048biological_processUDP-N-acetylglucosamine biosynthetic process
A0016853molecular_functionisomerase activity
A0016868molecular_functionintramolecular phosphotransferase activity
A0046349biological_processamino sugar biosynthetic process
A0046872molecular_functionmetal ion binding
A0071555biological_processcell wall organization
B0000287molecular_functionmagnesium ion binding
B0004610molecular_functionphosphoacetylglucosamine mutase activity
B0005975biological_processcarbohydrate metabolic process
B0006048biological_processUDP-N-acetylglucosamine biosynthetic process
B0016853molecular_functionisomerase activity
B0016868molecular_functionintramolecular phosphotransferase activity
B0046349biological_processamino sugar biosynthetic process
B0046872molecular_functionmetal ion binding
B0071555biological_processcell wall organization
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG A 998
ChainResidue
ASEP69
AASP284
AASP286
AASP288

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG B 998
ChainResidue
BSEP69
BASP284
BASP286
BASP288

Functional Information from PROSITE/UniProt
site_idPS00710
Number of Residues10
DetailsPGM_PMM Phosphoglucomutase and phosphomannomutase phosphoserine signature. GVmVTASHNP
ChainResidueDetails
AGLY63-PRO72

250359

PDB entries from 2026-03-11

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