1FRD

MOLECULAR STRUCTURE OF THE OXIDIZED, RECOMBINANT, HETEROCYST (2FE-2S) FERREDOXIN FROM ANABAENA 7120 DETERMINED TO 1.7 ANGSTROMS RESOLUTION

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0009055	molecular_function	electron transfer activity
A	0022900	biological_process	electron transport chain
A	0043158	biological_process	heterocyst development
A	0046872	molecular_function	metal ion binding
A	0051536	molecular_function	iron-sulfur cluster binding
A	0051537	molecular_function	2 iron, 2 sulfur cluster binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	8
Details	BINDING SITE FOR RESIDUE FES A 99

Chain	Residue
A	SER40
A	CYS41
A	HIS42
A	GLY44
A	SER45
A	CYS46
A	CYS49
A	CYS79

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Functional Information from PROSITE/UniProt

site_id	PS00197
Number of Residues	9
Details	2FE2S_FER_1 2Fe-2S ferredoxin-type iron-sulfur binding region signature. CHSGSCSSC

Chain	Residue	Details
A	CYS41-CYS49

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	92
Details	Domain: {"description":"2Fe-2S ferredoxin-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00465","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00465","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"8329401","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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