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4L36

Crystal structure of the cytochrome P450 enzyme TxtE

Functional Information from GO Data
ChainGOidnamespacecontents
A0004497molecular_functionmonooxygenase activity
A0005506molecular_functioniron ion binding
A0016491molecular_functionoxidoreductase activity
A0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
A0020037molecular_functionheme binding
A0046872molecular_functionmetal ion binding
B0004497molecular_functionmonooxygenase activity
B0005506molecular_functioniron ion binding
B0016491molecular_functionoxidoreductase activity
B0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
B0020037molecular_functionheme binding
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues24
DetailsBINDING SITE FOR RESIDUE HEB A 501
ChainResidue
AARG59
ASER254
ATHR296
AARG298
ALEU321
ASER349
APHE350
AGLY351
AVAL354
AHIS355
ACYS357
AVAL87
AALA359
AILE363
AIMD502
AHOH601
AHOH702
AMET88
AHIS95
AARG99
APHE155
AALA245
ATHR250
ATHR251

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE IMD A 502
ChainResidue
AALA245
AHEB501
AHOH738

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE IMD A 503
ChainResidue
ALEU73
APRO74
AASN77
AGLU187
BLEU73
BPRO74
BGLU187

site_idAC4
Number of Residues24
DetailsBINDING SITE FOR RESIDUE HEB B 501
ChainResidue
BARG59
BVAL87
BMET88
BHIS95
BARG99
BPHE155
BALA245
BTHR250
BTHR251
BSER254
BASN293
BTHR296
BARG298
BLEU321
BSER349
BPHE350
BGLY351
BVAL354
BHIS355
BCYS357
BALA359
BILE363
BIMD502
BHOH607

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE IMD B 502
ChainResidue
BMET88
BALA245
BTHR250
BHEB501

Functional Information from PROSITE/UniProt
site_idPS00086
Number of Residues10
DetailsCYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGqGVHACLA
ChainResidueDetails
APHE350-ALA359

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"25182183","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27102675","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4TPO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5D3U","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5D40","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"25182183","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27102675","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24282603","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"4L36","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4TPN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4TPO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5D3U","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5D40","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"27102675","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5D3U","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5D40","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsBinding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"25182183","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27102675","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24282603","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"4L36","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4TPN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4TPO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5D3U","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5D40","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

250359

PDB entries from 2026-03-11

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