8RON

Crystal structure of human FAD synthase, isoform 2

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0003919	molecular_function	FMN adenylyltransferase activity
A	0006747	biological_process	FAD biosynthetic process
B	0003824	molecular_function	catalytic activity
B	0003919	molecular_function	FMN adenylyltransferase activity
B	0006747	biological_process	FAD biosynthetic process
C	0003824	molecular_function	catalytic activity
C	0003919	molecular_function	FMN adenylyltransferase activity
C	0006747	biological_process	FAD biosynthetic process
D	0003824	molecular_function	catalytic activity
D	0003919	molecular_function	FMN adenylyltransferase activity
D	0006747	biological_process	FAD biosynthetic process

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976

Chain	Residue	Details
A	PRO203
B	PRO203
C	PRO203
D	PRO203

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site_id	SWS_FT_FI2
Number of Residues	4
Details	MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q8R123

Chain	Residue	Details
A	GLN475
B	GLN475
C	GLN475
D	GLN475

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