5ZBU

Crystal Structure of PA-TM-RING E3 ligase RNF13 RING domain in complex with E2~Ub

Functional Information from GO Data

Chain	GOid	namespace	contents
B	0000166	molecular_function	nucleotide binding
B	0000209	biological_process	protein polyubiquitination
B	0004842	molecular_function	ubiquitin-protein transferase activity
B	0005515	molecular_function	protein binding
B	0005524	molecular_function	ATP binding
B	0005634	cellular_component	nucleus
B	0005654	cellular_component	nucleoplasm
B	0005829	cellular_component	cytosol
B	0006511	biological_process	ubiquitin-dependent protein catabolic process
B	0016567	biological_process	protein ubiquitination
B	0016740	molecular_function	transferase activity
B	0032991	cellular_component	protein-containing complex
B	0036211	biological_process	protein modification process
B	0051865	biological_process	protein autoubiquitination
B	0061630	molecular_function	ubiquitin protein ligase activity
B	0061631	molecular_function	ubiquitin conjugating enzyme activity
B	0070062	cellular_component	extracellular exosome
B	0070936	biological_process	protein K48-linked ubiquitination
C	0000166	molecular_function	nucleotide binding
C	0000209	biological_process	protein polyubiquitination
C	0004842	molecular_function	ubiquitin-protein transferase activity
C	0005515	molecular_function	protein binding
C	0005524	molecular_function	ATP binding
C	0005634	cellular_component	nucleus
C	0005654	cellular_component	nucleoplasm
C	0005829	cellular_component	cytosol
C	0006511	biological_process	ubiquitin-dependent protein catabolic process
C	0016567	biological_process	protein ubiquitination
C	0016740	molecular_function	transferase activity
C	0032991	cellular_component	protein-containing complex
C	0036211	biological_process	protein modification process
C	0051865	biological_process	protein autoubiquitination
C	0061630	molecular_function	ubiquitin protein ligase activity
C	0061631	molecular_function	ubiquitin conjugating enzyme activity
C	0070062	cellular_component	extracellular exosome
C	0070936	biological_process	protein K48-linked ubiquitination

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	binding site for residue ZN A 1001

Chain	Residue
A	CYS240
A	CYS243
A	HIS263
A	CYS266

---

site_id	AC2
Number of Residues	4
Details	binding site for residue ZN A 1002

Chain	Residue
A	CYS258
A	HIS260
A	CYS278
A	CYS281

---

site_id	AC3
Number of Residues	4
Details	binding site for residue ZN D 1001

Chain	Residue
D	CYS243
D	HIS263
D	CYS266
D	CYS240

---

site_id	AC4
Number of Residues	4
Details	binding site for residue ZN D 1002

Chain	Residue
D	CYS258
D	HIS260
D	CYS278
D	CYS281

---

Functional Information from PROSITE/UniProt

site_id	PS00299
Number of Residues	26
Details	UBIQUITIN_1 Ubiquitin domain signature. KakIqDkegIPpdqQrLIFaGkqleD

Chain	Residue	Details
E	LYS27-ASP52

---

site_id	PS01186
Number of Residues	15
Details	EGF_2 EGF-like domain signature 2. CkCvdPWltktkkt.C

Chain	Residue	Details
A	CYS264-CYS278

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	146
Details	Domain: {"description":"UBC core","evidences":[{"source":"PROSITE-ProRule","id":"PRU00388","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	Active site: {"description":"Glycyl thioester intermediate","evidences":[{"source":"PROSITE-ProRule","id":"PRU00388","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10133","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	84
Details	Zinc finger: {"description":"RING-type; atypical","evidences":[{"source":"PROSITE-ProRule","id":"PRU00175","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	75
Details	Domain: {"description":"Ubiquitin-like 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00214","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---