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5Y5K

Time-resolved SFX structure of cytochrome P450nor : 20 ms after photo-irradiation of caged NO in the absence of NADH (NO-bound state), light data

Functional Information from GO Data
ChainGOidnamespacecontents
A0004497molecular_functionmonooxygenase activity
A0005506molecular_functioniron ion binding
A0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
A0020037molecular_functionheme binding
A0046872molecular_functionmetal ion binding
A0102199molecular_functionnitric oxide reductase (NAD(P)H) activity
B0004497molecular_functionmonooxygenase activity
B0005506molecular_functioniron ion binding
B0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
B0020037molecular_functionheme binding
B0046872molecular_functionmetal ion binding
B0102199molecular_functionnitric oxide reductase (NAD(P)H) activity
Functional Information from PDB Data
site_idAC1
Number of Residues22
Detailsbinding site for residue HEM A 501
ChainResidue
AVAL87
AGLY344
APHE345
AGLY346
APHE347
AHIS350
ACYS352
AILE353
AALA354
ANO502
AHOH606
AHIS94
AHOH657
AHOH719
AHOH746
AARG98
AILE153
ALEU236
AALA239
AGLY240
AMET244
AMET247

site_idAC2
Number of Residues3
Detailsbinding site for residue NO A 502
ChainResidue
AALA239
AHEM501
AHOH746

site_idAC3
Number of Residues22
Detailsbinding site for residue HEM B 501
ChainResidue
BPHE86
BVAL87
BHIS94
BARG98
BILE153
BLEU236
BGLY240
BMET244
BMET247
BGLY344
BPHE345
BGLY346
BPHE347
BHIS350
BCYS352
BILE353
BALA354
BNO502
BHOH601
BHOH607
BHOH643
BHOH725

site_idAC4
Number of Residues5
Detailsbinding site for residue NO B 502
ChainResidue
BALA239
BGLY240
BHEM501
BHOH679
BHOH725

Functional Information from PROSITE/UniProt
site_idPS00086
Number of Residues10
DetailsCYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGfGDHRCIA
ChainResidueDetails
APHE345-ALA354

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: axial binding residue
ChainResidueDetails
ACYS352
BCYS352

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: N-acetylalanine => ECO:0000269|PubMed:9010754
ChainResidueDetails
AALA2
BALA2

Catalytic Information from CSA
site_idMCSA1
Number of Residues4
DetailsM-CSA 473
ChainResidueDetails
ATHR243steric role
ASER286proton shuttle (general acid/base)
ACYS352activator, metal ligand
AASP393proton shuttle (general acid/base)

site_idMCSA2
Number of Residues4
DetailsM-CSA 473
ChainResidueDetails
BTHR243steric role
BSER286proton shuttle (general acid/base)
BCYS352activator, metal ligand
BASP393proton shuttle (general acid/base)

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PDB entries from 2024-10-30

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