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6EV9

Structure of E277D A. niger Fdc1 with prFMN in the hydroxylated form

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006744biological_processubiquinone biosynthetic process
A0008694molecular_function3-octaprenyl-4-hydroxybenzoate carboxy-lyase activity
A0009074biological_processaromatic amino acid family catabolic process
A0016831molecular_functioncarboxy-lyase activity
A0018966biological_processstyrene metabolic process
A0030145molecular_functionmanganese ion binding
A0033494biological_processferulate metabolic process
A0042802molecular_functionidentical protein binding
A0046281biological_processcinnamic acid catabolic process
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues7
Detailsbinding site for residue MN A 601
ChainResidue
AASN168
AHIS191
AGLU233
AK602
ABYN604
AHOH796
AHOH802

site_idAC2
Number of Residues7
Detailsbinding site for residue K A 602
ChainResidue
ASER223
AMET225
AGLU233
AMN601
ABYN604
ATRP169
AALA222

site_idAC3
Number of Residues6
Detailsbinding site for residue K A 603
ChainResidue
AARG421
AASP427
AASP459
ALEU461
AHOH982
AHOH1099

site_idAC4
Number of Residues24
Detailsbinding site for residue BYN A 604
ChainResidue
ATHR153
AASN168
ASER170
AILE171
AALA172
AARG173
AGLN190
AHIS191
ASER223
ASER224
AMET225
APRO226
AGLU233
AGLU282
AILE327
ALYS391
AMN601
AK602
AHOH730
AHOH802
AHOH803
AHOH813
AHOH881
AHOH944

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_03196, ECO:0000305|PubMed:26083754
ChainResidueDetails
AGLU282

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03196, ECO:0000269|PubMed:26083754
ChainResidueDetails
ALYS391
AASN168
AGLN190
AHIS191

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03196
ChainResidueDetails
AGLU233

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PDB entries from 2024-06-12

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