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3V48

Crystal Structure of the putative alpha/beta hydrolase RutD from E.coli

Functional Information from GO Data
ChainGOidnamespacecontents
A0006212biological_processuracil catabolic process
A0016787molecular_functionhydrolase activity
A0016811molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
A0019740biological_processnitrogen utilization
B0006212biological_processuracil catabolic process
B0016787molecular_functionhydrolase activity
B0016811molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
B0019740biological_processnitrogen utilization
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 267
ChainResidue
AGLY23
AHIS87
ALEU148
ASCN270
AHOH296
AHOH349
AHOH407

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 268
ChainResidue
AALA158
ALEU161
AHOH357
AHOH415
BHIS120
BARG123
BHOH449
AMSE154
AALA155

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SCN A 269
ChainResidue
AGLY23
AARG128
ATRP140
AGLN144
AHOH294

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SCN A 270
ChainResidue
ALEU22
AALA88
ALEU89
ALEU185
ALEU211
AHIS237
AGOL267
AHOH294

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL B 267
ChainResidue
BGLY21
BLEU22
BGLY23
BHIS87
BHOH270
BHOH283
BHOH416

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL B 268
ChainResidue
AHIS120
AARG123
BMSE154
BALA155
BALA158

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SCN B 269
ChainResidue
AHIS0
AARG48
BARG157
BPRO159
BARG160

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PDB entries from 2024-08-21

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