6EV7

Structure of E282D A. niger Fdc1 with prFMN in the iminium form

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005737	cellular_component	cytoplasm
A	0009074	biological_process	aromatic amino acid family catabolic process
A	0016831	molecular_function	carboxy-lyase activity
A	0018966	biological_process	styrene metabolic process
A	0030145	molecular_function	manganese ion binding
A	0033494	biological_process	ferulate metabolic process
A	0042802	molecular_function	identical protein binding
A	0046281	biological_process	cinnamic acid catabolic process
A	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	binding site for residue MN A 601

Chain	Residue
A	ASN168
A	HIS191
A	GLU233
A	K602
A	4LU604
A	HOH734
A	HOH855

---

site_id	AC2
Number of Residues	7
Details	binding site for residue K A 602

Chain	Residue
A	SER223
A	MET225
A	GLU233
A	MN601
A	4LU604
A	TRP169
A	ALA222

---

site_id	AC3
Number of Residues	6
Details	binding site for residue K A 603

Chain	Residue
A	ARG421
A	ASP427
A	ASP459
A	LEU461
A	HOH966
A	HOH1183

---

site_id	AC4
Number of Residues	26
Details	binding site for residue 4LU A 604

Chain	Residue
A	THR153
A	ASN168
A	SER170
A	ILE171
A	ALA172
A	ARG173
A	LEU185
A	GLN190
A	HIS191
A	SER223
A	SER224
A	MET225
A	PRO226
A	GLU233
A	ASP282
A	ILE327
A	LYS391
A	MN601
A	K602
A	HOH734
A	HOH777
A	HOH786
A	HOH790
A	HOH811
A	HOH963
A	HOH1127

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_03196, ECO:0000305|PubMed:26083754

Chain	Residue	Details
A	ASP282

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03196, ECO:0000269|PubMed:26083754

Chain	Residue	Details
A	ASN168
A	GLN190
A	HIS191
A	LYS391

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03196

Chain	Residue	Details
A	GLU233

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