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6FV3

Crystal structure of N-acetyl-D-glucosamine-6-phosphate deacetylase from Mycobacterium smegmatis.

Functional Information from GO Data
ChainGOidnamespacecontents
A0006040biological_processamino sugar metabolic process
A0006044biological_processN-acetylglucosamine metabolic process
A0008448molecular_functionN-acetylglucosamine-6-phosphate deacetylase activity
A0016787molecular_functionhydrolase activity
A0016810molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
A0046872molecular_functionmetal ion binding
A0047419molecular_functionN-acetylgalactosamine-6-phosphate deacetylase activity
B0006040biological_processamino sugar metabolic process
B0006044biological_processN-acetylglucosamine metabolic process
B0008448molecular_functionN-acetylglucosamine-6-phosphate deacetylase activity
B0016787molecular_functionhydrolase activity
B0016810molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
B0046872molecular_functionmetal ion binding
B0047419molecular_functionN-acetylgalactosamine-6-phosphate deacetylase activity
C0006040biological_processamino sugar metabolic process
C0006044biological_processN-acetylglucosamine metabolic process
C0008448molecular_functionN-acetylglucosamine-6-phosphate deacetylase activity
C0016787molecular_functionhydrolase activity
C0016810molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
C0046872molecular_functionmetal ion binding
C0047419molecular_functionN-acetylgalactosamine-6-phosphate deacetylase activity
D0006040biological_processamino sugar metabolic process
D0006044biological_processN-acetylglucosamine metabolic process
D0008448molecular_functionN-acetylglucosamine-6-phosphate deacetylase activity
D0016787molecular_functionhydrolase activity
D0016810molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
D0046872molecular_functionmetal ion binding
D0047419molecular_functionN-acetylgalactosamine-6-phosphate deacetylase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue ZN A 401
ChainResidue
AHIS56
AHIS58
AGLU122
AASP267
AZN402
AHOH539

site_idAC2
Number of Residues6
Detailsbinding site for residue ZN A 402
ChainResidue
AZN401
AHOH539
AHOH572
AGLU122
AHIS188
AHIS209

site_idAC3
Number of Residues6
Detailsbinding site for residue ZN B 401
ChainResidue
BHIS56
BHIS58
BGLU122
BASP267
BZN402
BHOH526

site_idAC4
Number of Residues6
Detailsbinding site for residue ZN B 402
ChainResidue
BGLU122
BHIS188
BHIS209
BZN401
BHOH526
BHOH563

site_idAC5
Number of Residues6
Detailsbinding site for residue ZN C 401
ChainResidue
CHIS56
CHIS58
CGLU122
CASP267
CHOH510
CHOH530

site_idAC6
Number of Residues5
Detailsbinding site for residue ZN C 402
ChainResidue
CGLU122
CHIS188
CHIS209
CHOH510
CHOH576

site_idAC7
Number of Residues6
Detailsbinding site for residue ZN D 401
ChainResidue
DHIS56
DHIS58
DGLU122
DASP267
DZN402
DHOH524

site_idAC8
Number of Residues6
Detailsbinding site for residue ZN D 402
ChainResidue
DGLU122
DHIS188
DHIS209
DZN401
DHOH524
DHOH572

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PDB entries from 2024-07-17

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