4IOU

Crystal structure of the HIV-1 Vif binding, catalytically active domain of APOBEC3F

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0008270	molecular_function	zinc ion binding
A	0016787	molecular_function	hydrolase activity
B	0003824	molecular_function	catalytic activity
B	0008270	molecular_function	zinc ion binding
B	0016787	molecular_function	hydrolase activity
C	0003824	molecular_function	catalytic activity
C	0008270	molecular_function	zinc ion binding
C	0016787	molecular_function	hydrolase activity
D	0003824	molecular_function	catalytic activity
D	0008270	molecular_function	zinc ion binding
D	0016787	molecular_function	hydrolase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE ZN A 1001

Chain	Residue
A	HIS249
A	CYS280
A	CYS283

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site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE ZN B 1001

Chain	Residue
B	HIS249
B	CYS280
B	CYS283

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site_id	AC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE ZN C 1001

Chain	Residue
C	HIS249
C	CYS280
C	CYS283

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site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN D 1001

Chain	Residue
D	HIS249
D	CYS280
D	CYS283
D	HOH1108

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Functional Information from PROSITE/UniProt

site_id	PS00903
Number of Residues	39
Details	CYT_DCMP_DEAMINASES_1 Cytidine and deoxycytidylate deaminases zinc-binding region signature. HAErcFLswfaddilspntnyevtwytsws..........PCpe......CageV

Chain	Residue	Details
A	HIS249-VAL287

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU01083

Chain	Residue	Details
A	GLU251
B	GLU251
C	GLU251
D	GLU251

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site_id	SWS_FT_FI2
Number of Residues	12
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01083, ECO:0000269|PubMed:27139641

Chain	Residue	Details
A	HIS249
D	HIS249
D	CYS280
D	CYS283
A	CYS280
A	CYS283
B	HIS249
B	CYS280
B	CYS283
C	HIS249
C	CYS280
C	CYS283

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