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3VEW

Crystal structure of the O-carbamoyltransferase TobZ in complex with ADP

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0005506molecular_functioniron ion binding
A0005524molecular_functionATP binding
A0009058biological_processbiosynthetic process
A0016743molecular_functioncarboxyl- or carbamoyltransferase activity
A0016787molecular_functionhydrolase activity
A0016874molecular_functionligase activity
A0017000biological_processantibiotic biosynthetic process
A0046872molecular_functionmetal ion binding
A1901121biological_processtobramycin biosynthetic process
A1901133biological_processkanamycin biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues20
DetailsBINDING SITE FOR RESIDUE ADP A 601
ChainResidue
AHIS14
APRO185
ALEU285
AGLY310
AVAL311
AASN314
ASER337
AASP338
AFE2602
AHOH757
AHOH787
AHIS114
AHOH803
AHIS118
AASP137
AGLY138
AGLN139
AGLY168
ATYR171
AGLU172

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE2 A 602
ChainResidue
AHIS114
AHIS118
AASP137
AASP338
AADP601

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 603
ChainResidue
AARG418
AARG445
ATHR529
ASER530
AHOH754
AHOH776
AHOH797

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000305|PubMed:22383337
ChainResidueDetails
AHIS14

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

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
AASN314
AGLN139
AGLY168
AGLY310

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PDB entries from 2024-05-29

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