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7Q04

Crystal structure of TPADO in a substrate-free state

Functional Information from GO Data
ChainGOidnamespacecontents
A0005506molecular_functioniron ion binding
A0016491molecular_functionoxidoreductase activity
A0018628molecular_functionterephthalate 1,2-dioxygenase activity
A0018963biological_processphthalate metabolic process
A0051213molecular_functiondioxygenase activity
B0005506molecular_functioniron ion binding
B0016491molecular_functionoxidoreductase activity
B0018628molecular_functionterephthalate 1,2-dioxygenase activity
B0018963biological_processphthalate metabolic process
B0051213molecular_functiondioxygenase activity
C0005506molecular_functioniron ion binding
C0016491molecular_functionoxidoreductase activity
C0018628molecular_functionterephthalate 1,2-dioxygenase activity
C0018963biological_processphthalate metabolic process
C0051213molecular_functiondioxygenase activity
D0005506molecular_functioniron ion binding
D0016491molecular_functionoxidoreductase activity
D0018628molecular_functionterephthalate 1,2-dioxygenase activity
D0018963biological_processphthalate metabolic process
D0046872molecular_functionmetal ion binding
D0051213molecular_functiondioxygenase activity
D0051536molecular_functioniron-sulfur cluster binding
D0051537molecular_function2 iron, 2 sulfur cluster binding
E0005506molecular_functioniron ion binding
E0016491molecular_functionoxidoreductase activity
E0018628molecular_functionterephthalate 1,2-dioxygenase activity
E0018963biological_processphthalate metabolic process
E0046872molecular_functionmetal ion binding
E0051213molecular_functiondioxygenase activity
E0051536molecular_functioniron-sulfur cluster binding
E0051537molecular_function2 iron, 2 sulfur cluster binding
F0005506molecular_functioniron ion binding
F0016491molecular_functionoxidoreductase activity
F0018628molecular_functionterephthalate 1,2-dioxygenase activity
F0018963biological_processphthalate metabolic process
F0046872molecular_functionmetal ion binding
F0051213molecular_functiondioxygenase activity
F0051536molecular_functioniron-sulfur cluster binding
F0051537molecular_function2 iron, 2 sulfur cluster binding
H0003796molecular_functionlysozyme activity
H0003824molecular_functioncatalytic activity
H0005515molecular_functionprotein binding
H0005576cellular_componentextracellular region
H0005615cellular_componentextracellular space
H0005737cellular_componentcytoplasm
H0005783cellular_componentendoplasmic reticulum
H0016231molecular_functionbeta-N-acetylglucosaminidase activity
H0016787molecular_functionhydrolase activity
H0016798molecular_functionhydrolase activity, acting on glycosyl bonds
H0016998biological_processcell wall macromolecule catabolic process
H0031640biological_processkilling of cells of another organism
H0042742biological_processdefense response to bacterium
H0042802molecular_functionidentical protein binding
H0050829biological_processdefense response to Gram-negative bacterium
H0050830biological_processdefense response to Gram-positive bacterium
H0051672biological_processobsolete catabolism by organism of cell wall peptidoglycan in other organism
Functional Information from PROSITE/UniProt
site_idPS00128
Number of Residues19
DetailsGLYCOSYL_HYDROL_F22_1 Glycosyl hydrolases family 22 (GH22) domain signature. CnipCsaLlssDItasvnC
ChainResidueDetails
HCYS76-CYS94

site_idPS00570
Number of Residues24
DetailsRING_HYDROXYL_ALPHA Bacterial ring hydroxylating dioxygenases alpha-subunit signature. CaHRGalialeksGRtdsfqCvYH
ChainResidueDetails
DCYS82-HIS105

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues309
DetailsDomain: {"description":"Rieske","evidences":[{"source":"PROSITE-ProRule","id":"PRU00628","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00628","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues128
DetailsDomain: {"description":"C-type lysozyme","evidences":[{"source":"PROSITE-ProRule","id":"PRU00680","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsActive site: {}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsBinding site: {}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues6
DetailsM-CSA 203
ChainResidueDetails

240971

PDB entries from 2025-08-27

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