Structure of PDB 1rz1 Chain D

Receptor sequence
>1rz1D (length=153) Species: 1426 (Parageobacillus thermoglucosidasius) [Search protein sequence]
MDDRLFRNAMGKFATGVTVITTELNGAVHGMTANAFMSVSLNPKLVLVSI
GEKAKMLEKIQQSKKYAVNILSQDQKVLSMNFAGQLEKPVDVQFEELGGL
PVIKDALAQISCQVVNEVQAGDHTLFIGEVTDIKITEQDPLLFFSGKYHQ
LAQ
3D structure
PDB1rz1 Structural Studies on Flavin Reductase PheA2 Reveal Binding of NAD in an Unusual Folded Conformation and Support Novel Mechanism of Action.
ChainD
Resolution2.1 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Enzyme Commision number ?
Interaction with ligand
Site
#
Ligand Ligand
chain
Binding residues on receptor
(original residue number in PDB)
Binding residues on receptor
(residue number reindexed from 1)
Binding affinity
BS01 FAD D V28 G30 M31 T32 A33 N34 A35 A54 K55 M56 N81 F82 A83 G84 V28 G30 M31 T32 A33 N34 A35 A54 K55 M56 N81 F82 A83 G84 MOAD: Kd=9.8nM
BS02 NAD D R7 M10 G11 N34 H123 F143 R7 M10 G11 N34 H123 F143
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0010181 FMN binding
GO:0016646 oxidoreductase activity, acting on the CH-NH group of donors, NAD or NADP as acceptor
GO:0042602 riboflavin reductase (NADPH) activity
Biological Process
GO:0006208 pyrimidine nucleobase catabolic process

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:1rz1, PDBe:1rz1, PDBj:1rz1
PDBsum1rz1
PubMed14703520
UniProtQ9LAG2

[Back to BioLiP]