9J7L

Structure of AAV8 capsid in complex with receptor

This is a non-PDB format compatible entry.

Functional Information from GO Data

Chain	GOid	namespace	contents
5	0000166	molecular_function	nucleotide binding
5	0019028	cellular_component	viral capsid
5	0039615	cellular_component	T=1 icosahedral viral capsid
5	0044423	cellular_component	virion component
6	0000166	molecular_function	nucleotide binding
6	0019028	cellular_component	viral capsid
6	0039615	cellular_component	T=1 icosahedral viral capsid
6	0044423	cellular_component	virion component
7	0000166	molecular_function	nucleotide binding
7	0019028	cellular_component	viral capsid
7	0039615	cellular_component	T=1 icosahedral viral capsid
7	0044423	cellular_component	virion component
c	0000166	molecular_function	nucleotide binding
c	0019028	cellular_component	viral capsid
c	0039615	cellular_component	T=1 icosahedral viral capsid
c	0044423	cellular_component	virion component
o	0000166	molecular_function	nucleotide binding
o	0019028	cellular_component	viral capsid
o	0039615	cellular_component	T=1 icosahedral viral capsid
o	0044423	cellular_component	virion component
p	0000166	molecular_function	nucleotide binding
p	0019028	cellular_component	viral capsid
p	0039615	cellular_component	T=1 icosahedral viral capsid
p	0044423	cellular_component	virion component

Functional Information from PROSITE/UniProt

site_id	PS00132
Number of Residues	23
Details	CARBOXYPEPT_ZN_1 Zinc carboxypeptidases, zinc-binding region 1 signature. PqVkLvgNmHGdEtVSRqvliyL

Chain	Residue	Details
A	PRO130-LEU152

---

site_id	PS00133
Number of Residues	11
Details	CARBOXYPEPT_ZN_2 Zinc carboxypeptidases, zinc-binding region 2 signature. HGGSVVAsYPF

Chain	Residue	Details
A	HIS257-PHE267

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI2
Number of Residues	1
Details	Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU01379","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	3
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01379","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"O89001","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"O89001","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"12754519","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	4
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---