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3VEZ

Crystal structure of the O-carbamoyltransferase TobZ K443A variant in complex with ATP, ADP and carbamoyl phosphate

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 Residues5
DetailsBINDING SITE FOR RESIDUE FE2 A 601
ChainResidue
AHIS114
AHIS118
AASP137
AASP338
AADP603

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 602
ChainResidue
AHOH965
AHOH966
ASER530
AATP604
ACP605
AHOH851

site_idAC3
Number of Residues20
DetailsBINDING SITE FOR RESIDUE ADP A 603
ChainResidue
AHIS14
AHIS114
AHIS118
AASP137
AGLY138
AGLN139
AGLY168
APHE169
ATYR171
AGLU172
APRO185
AGLY310
AVAL311
ALEU313
AASN314
ASER337
AASP338
AFE2601
AHOH775
AHOH804

site_idAC4
Number of Residues20
DetailsBINDING SITE FOR RESIDUE ATP A 604
ChainResidue
ALYS39
AGLY186
AMET189
AGLY190
ATHR316
AARG418
AARG449
APRO450
AHIS492
ASER496
AARG498
AASN532
AMG602
ACP605
AHOH761
AHOH799
AHOH809
AHOH851
AHOH860
AHOH966

site_idAC5
Number of Residues12
DetailsBINDING SITE FOR RESIDUE CP A 605
ChainResidue
AARG418
AALA419
AARG445
AMET473
AARG498
AASN528
ATHR529
ASER530
AMG602
AATP604
AHOH711
AHOH966

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE K A 606
ChainResidue
ALEU322
AARG324
AVAL327

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
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 2024-09-11

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