4LDT

The structure of h/ceOTUB1-ubiquitin aldehyde-UBCH5B~Ub

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0016579	biological_process	protein deubiquitination
A	0016787	molecular_function	hydrolase activity
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 EDO A 301

Chain	Residue
A	MET101
A	LEU102
A	ARG105
A	ILE146

---

site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE EDO A 302

Chain	Residue
A	ALA155
A	THR158
A	HOH492

---

site_id	AC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE EDO A 303

Chain	Residue
A	GLU194
A	TYR201
A	ASP214
A	LEU216
A	HOH450
A	HOH482
A	ILE192
A	ASP193

---

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG B 101

Chain	Residue
B	ASP32
B	HOH220
B	HOH221
B	HOH222
B	HOH227

---

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO C 201

Chain	Residue
C	MET38
C	GLY39
C	GLN46
C	GLY47
C	GLY48

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
D	LYS27-ASP52
B	LYS27-ASP52

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	16
Details	Region: {"description":"Ubiquitin-conjugating enzyme E2 binding","evidences":[{"source":"PubMed","id":"22325355","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	13
Details	Region: {"description":"Free ubiquitin binding","evidences":[{"source":"PubMed","id":"22325355","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22367539","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4DHZ","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	7
Details	Region: {"description":"Ubiquitin-conjugating enzyme E2 binding","evidences":[{"source":"PubMed","id":"22325355","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22367539","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4DHZ","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	Active site: {"evidences":[{"source":"UniProtKB","id":"Q96DC9","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	Active site: {"description":"Nucleophile","evidences":[{"source":"UniProtKB","id":"Q96DC9","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	Site: {"description":"Required for proximal ubiquitin-binding","evidences":[{"source":"PubMed","id":"19211026","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	4
Details	Site: {"description":"Interacts with free ubiquitin","evidences":[{"source":"PubMed","id":"22325355","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	1
Details	Site: {"description":"Interacts with free ubiquitin","evidences":[{"source":"PubMed","id":"22325355","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22367539","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4DHZ","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI9
Number of Residues	1
Details	Modified residue: {"description":"Phosphotyrosine; by SRC","evidences":[{"source":"PubMed","id":"35927303","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI10
Number of Residues	1
Details	Active site: {"evidences":[{"source":"UniProtKB","id":"Q96FW1","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI11
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"Q5VVQ6","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI12
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_FI13
Number of Residues	1
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_FI14
Number of Residues	75
Details	Domain: {"description":"Ubiquitin-like 9","evidences":[{"source":"PROSITE-ProRule","id":"PRU00214","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---