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6EVD

Structure of R173A A. niger Fdc1 with prFMN in the hydroxylated form

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
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
ABYN603
AHOH756
AHOH833

site_idAC2
Number of Residues7
Detailsbinding site for residue K A 602
ChainResidue
ASER223
AMET225
AGLU233
AMN601
ABYN603
ATRP169
AALA222

site_idAC3
Number of Residues26
Detailsbinding site for residue BYN A 603
ChainResidue
ATHR153
AASN168
ASER170
AILE171
AALA172
AALA173
AGLN190
AHIS191
ASER223
ASER224
AMET225
APRO226
AGLU233
AGLU282
AILE327
ALYS391
AMN601
AK602
AHOH756
AHOH799
AHOH815
AHOH817
AHOH825
AHOH828
AHOH1053
AHOH1150

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
AASN168
AGLN190
AHIS191
ALYS391

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

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PDB entries from 2024-07-10

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