1FCA

STRUCTURE OF THE FERREDOXIN FROM CLOSTRIDIUM ACIDURICI: MODEL AT 1.8 ANGSTROMS RESOLUTION

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005737	cellular_component	cytoplasm
A	0009055	molecular_function	electron transfer activity
A	0046872	molecular_function	metal ion binding
A	0051536	molecular_function	iron-sulfur cluster binding
A	0051539	molecular_function	4 iron, 4 sulfur cluster binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SF4 A 56

Chain	Residue
A	ILE9
A	CYS11
A	GLY12
A	CYS14
A	TYR30
A	CYS47
A	VAL49
A	CYS8

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site_id	AC2
Number of Residues	10
Details	BINDING SITE FOR RESIDUE SF4 A 57

Chain	Residue
A	TYR2
A	CYS18
A	VAL20
A	ILE23
A	CYS37
A	ILE38
A	CYS40
A	GLY41
A	ALA42
A	CYS43

---

site_id	FS4
Number of Residues	8
Details

Chain	Residue
A	CYS8
A	CYS11
A	CYS14
A	CYS47
A	CYS18
A	CYS37
A	CYS40
A	CYS43

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Functional Information from PROSITE/UniProt

site_id	PS00198
Number of Residues	12
Details	4FE4S_FER_1 4Fe-4S ferredoxin-type iron-sulfur binding region signature. CiSCGaCEpECP

Chain	Residue	Details
A	CYS8-PRO19
A	CYS37-PRO48

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	27
Details	Domain: {"description":"4Fe-4S ferredoxin-type 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00711","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00711","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"7966291","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9405040","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1FDN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2FDN","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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