1RTT

Crystal structure determination of a putative NADH-dependent reductase using sulfur anomalous signal

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0003955	molecular_function	NAD(P)H dehydrogenase (quinone) activity
A	0005829	cellular_component	cytosol
A	0010181	molecular_function	FMN binding
A	0016491	molecular_function	oxidoreductase activity
A	0016655	molecular_function	oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor
A	0042802	molecular_function	identical protein binding
A	0042803	molecular_function	protein homodimerization activity
A	0052873	molecular_function	FMN reductase (NADPH) activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 A 194

Chain	Residue
A	SER15
A	ARG17
A	SER20
A	TYR21
A	ASN22
A	HOH207

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	9
Details	Binding site: {"evidences":[{"source":"PubMed","id":"16552139","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	7
Details	Binding site: {"evidences":[{"source":"PubMed","id":"16552139","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

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