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5Y5J

Time-resolved SFX structure of cytochrome P450nor: dark-2 data in the presence of NADH (resting state)

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 Residues25
Detailsbinding site for residue HEM A 501
ChainResidue
APHE86
AMET247
ASER286
AALA289
AGLY344
APHE345
AGLY346
APHE347
AHIS350
ACYS352
AILE353
AVAL87
AALA354
AGOL502
AHOH609
AHOH669
AHOH681
AHOH724
AHIS94
AARG98
AILE153
ALEU236
AALA239
AGLY240
AMET244

site_idAC2
Number of Residues6
Detailsbinding site for residue GOL A 502
ChainResidue
AVAL87
AALA239
AALA289
AHEM501
AHOH679
AHOH724

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
BGOL502
BHOH602
BHOH609
BHOH619
BHOH700

site_idAC4
Number of Residues6
Detailsbinding site for residue GOL B 502
ChainResidue
BVAL87
BALA239
BSER286
BALA289
BHEM501
BHOH700

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 2024-09-18

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