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4QNW

Crystal structure of EasA, an old yellow enzyme from Aspergillus fumigatus

Functional Information from GO Data
ChainGOidnamespacecontents
A0003959molecular_functionNADPH dehydrogenase activity
A0009820biological_processalkaloid metabolic process
A0010181molecular_functionFMN binding
A0016491molecular_functionoxidoreductase activity
A0016646molecular_functionoxidoreductase activity, acting on the CH-NH group of donors, NAD or NADP as acceptor
A0035835biological_processindole alkaloid biosynthetic process
A0035837biological_processergot alkaloid biosynthetic process
A1900809biological_processfumigaclavine C biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues22
DetailsBINDING SITE FOR RESIDUE FMN A 401
ChainResidue
AALA28
AGLY296
AGLY297
APHE322
AGLY323
AARG324
AASN373
APHE374
AHOH527
AHOH529
AHOH532
APRO29
AHOH554
AHOH702
AHOH723
ATHR30
ATHR31
AALA64
AGLN106
AHIS173
AASN176
ALYS225

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 402
ChainResidue
ALYS100
ALYS344
AASP346
AARG347

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 403
ChainResidue
ALYS186
AMET238
AASP239
AHOH543
AHOH583

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 404
ChainResidue
ALYS186
AGLY197
AARG202
AHOH662

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 A 405
ChainResidue
AARG160
AARG221

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 406
ChainResidue
AGLN149
AARG194
AGLU208
AHOH578

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000250
ChainResidueDetails
ATYR178

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:25286934
ChainResidueDetails
APRO29
AALA64
AGLN106
ALYS225
AGLY297
AGLY323

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q02899
ChainResidueDetails
AHIS173
AASN176
AARG324
ATYR351

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PDB entries from 2024-07-17

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