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6EV5

Crystal structure of E282Q 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
ABYN604
AHOH752
AHOH867

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
AHOH1015
AHOH1148

site_idAC4
Number of Residues26
Detailsbinding site for residue BYN A 604
ChainResidue
ATHR153
AASN168
ASER170
AILE171
AALA172
AARG173
ALEU185
AGLN190
AHIS191
ASER223
ASER224
AMET225
APRO226
AGLU233
AILE327
ALYS391
AMN601
AK602
ASCN605
AHOH752
AHOH775
AHOH802
AHOH865
AHOH882
AHOH1031
AHOH1035

site_idAC5
Number of Residues5
Detailsbinding site for residue SCN A 605
ChainResidue
AARG173
APHE280
AGLN282
AMET283
ABYN604

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
AGLN282

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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