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3VEX

Crystal structure of the O-carbamoyltransferase TobZ H14N variant in complex with carbamoyl adenylate intermediate

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003824molecular_functioncatalytic activity
A0005506molecular_functioniron ion binding
A0005524molecular_functionATP binding
A0009058biological_processbiosynthetic process
A0016138biological_processglycoside biosynthetic process
A0016743molecular_functioncarboxyl- or carbamoyltransferase activity
A0016787molecular_functionhydrolase activity
A0016874molecular_functionligase activity
A0017000biological_processantibiotic biosynthetic process
A0044281biological_processsmall molecule metabolic process
A0046872molecular_functionmetal ion binding
A1901121biological_processtobramycin biosynthetic process
A1901133biological_processkanamycin biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE2 A 601
ChainResidue
AHIS114
AHIS118
AASP137
AASP338
ACA0602

site_idAC2
Number of Residues20
DetailsBINDING SITE FOR RESIDUE CA0 A 602
ChainResidue
AGLN139
AGLY168
APHE169
ATYR171
AGLU172
APRO185
AGLY310
AVAL311
AASN314
ASER337
AASP338
AFE2601
AHOH1169
AHOH1235
AHOH1379
AHOH1403
AHIS114
AHIS118
AASP137
AGLY138

site_idAC3
Number of Residues12
DetailsBINDING SITE FOR RESIDUE SO4 A 603
ChainResidue
AARG445
APHE451
AARG498
ATHR529
ASER530
AHOH712
AHOH897
AHOH912
AHOH1087
AHOH1193
AHOH1195
AHOH1400

site_idAC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 A 604
ChainResidue
AARG449
AASN532
AARG534
AGLY535
AHOH1096
AHOH1151
AHOH1160
AHOH1196
AHOH1365

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 605
ChainResidue
AARG435
APRO450
APHE451
APRO488
ASER489
AVAL491

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 606
ChainResidue
AGLY153
AASP355
AARG356
AILE357

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 607
ChainResidue
ASER209
AGLY403
ASER431
ATHR433

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000305|PubMed:22383337
ChainResidueDetails
AASN14

site_idSWS_FT_FI2
Number of Residues9
DetailsBINDING: BINDING => ECO:0000269|PubMed:22383337, ECO:0007744|PDB:3VET
ChainResidueDetails
AASP12
AHIS114
AHIS118
AASP137
AGLU172
AASP228
AASP338
AARG498
AASN528

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:22383337, ECO:0007744|PDB:3VEZ
ChainResidueDetails
ALYS39
AARG418
AARG449

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:22383337, ECO:0007744|PDB:3VEX
ChainResidueDetails
AGLN139
AGLY168
AGLY310
AASN314

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PDB entries from 2025-06-18

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