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3GIQ

Crystal structure of N-acyl-D-Glutamate Deacylase from Bordetella Bronchiseptica complexed with zinc and phosphonate inhibitor, a mimic of the reaction tetrahedral intermediate.

Functional Information from GO Data
ChainGOidnamespacecontents
A0016787molecular_functionhydrolase activity
A0016810molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
A0016811molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
A0046872molecular_functionmetal ion binding
A0047421molecular_functionN-acyl-D-glutamate deacylase activity
B0016787molecular_functionhydrolase activity
B0016810molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
B0016811molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
B0046872molecular_functionmetal ion binding
B0047421molecular_functionN-acyl-D-glutamate deacylase activity
Functional Information from PDB Data
site_idAC1
Number of Residues18
DetailsBINDING SITE FOR RESIDUE G01 A 481
ChainResidue
AHIS66
ATYR282
ASER287
ASER288
AARG295
AASP365
AARG376
AZN482
AZN483
AHOH522
AHIS68
ACYS95
ATYR190
AHIS218
AGLU222
AHIS248
ALYS250
AMET252

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 482
ChainResidue
ACYS95
AHIS218
AHIS248
AG01481
AZN483

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN A 483
ChainResidue
AHIS66
AHIS68
ACYS95
AASP365
AG01481
AZN482

site_idAC4
Number of Residues18
DetailsBINDING SITE FOR RESIDUE G01 B 481
ChainResidue
BHIS66
BHIS68
BCYS95
BTYR190
BHIS218
BGLU222
BHIS248
BLYS250
BMET252
BTYR282
BSER287
BSER288
BARG295
BASP365
BARG376
BZN482
BZN483
BHOH495

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN B 482
ChainResidue
BCYS95
BHIS218
BHIS248
BG01481
BZN483

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN B 483
ChainResidue
BHIS66
BHIS68
BCYS95
BASP365
BG01481
BZN482

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PDB entries from 2024-10-30

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