5CAW

Structure of Pediculus humanus Parkin bound to phospho-ubiquitin

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004842	molecular_function	ubiquitin-protein transferase activity
A	0005739	cellular_component	mitochondrion
A	0005829	cellular_component	cytosol
A	0008270	molecular_function	zinc ion binding
A	0016567	biological_process	protein ubiquitination
C	0004842	molecular_function	ubiquitin-protein transferase activity
C	0005739	cellular_component	mitochondrion
C	0005829	cellular_component	cytosol
C	0008270	molecular_function	zinc ion binding
C	0016567	biological_process	protein ubiquitination

Functional Information from PDB Data

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

Chain	Residue
A	CYS151
A	CYS155
A	CYS213
A	HIS216

---

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

Chain	Residue
A	CYS167
A	CYS170
A	CYS197
A	CYS202

---

site_id	AC3
Number of Residues	4
Details	binding site for residue ZN A 1003

Chain	Residue
A	CYS243
A	CYS262
A	CYS265
A	CYS240

---

site_id	AC4
Number of Residues	4
Details	binding site for residue ZN A 1004

Chain	Residue
A	CYS255
A	HIS259
A	CYS291
A	CYS295

---

site_id	AC5
Number of Residues	4
Details	binding site for residue ZN A 1005

Chain	Residue
A	CYS334
A	CYS339
A	CYS354
A	CYS356

---

site_id	AC6
Number of Residues	4
Details	binding site for residue ZN A 1006

Chain	Residue
A	CYS361
A	CYS364
A	HIS369
A	CYS373

---

site_id	AC7
Number of Residues	4
Details	binding site for residue ZN A 1007

Chain	Residue
A	CYS415
A	CYS418
A	CYS433
A	CYS438

---

site_id	AC8
Number of Residues	4
Details	binding site for residue ZN A 1008

Chain	Residue
A	CYS443
A	CYS446
A	CYS454
A	HIS458

---

site_id	AC9
Number of Residues	4
Details	binding site for residue SO4 A 1009

Chain	Residue
A	SER183
A	TRP184
A	ARG258
A	HOH1104

---

site_id	AD1
Number of Residues	4
Details	binding site for residue ZN C 1001

Chain	Residue
C	CYS151
C	CYS155
C	CYS213
C	HIS216

---

site_id	AD2
Number of Residues	4
Details	binding site for residue ZN C 1002

Chain	Residue
C	CYS167
C	CYS170
C	CYS197
C	CYS202

---

site_id	AD3
Number of Residues	4
Details	binding site for residue ZN C 1003

Chain	Residue
C	CYS240
C	CYS243
C	CYS262
C	CYS265

---

site_id	AD4
Number of Residues	4
Details	binding site for residue ZN C 1004

Chain	Residue
C	CYS255
C	HIS259
C	CYS291
C	CYS295

---

site_id	AD5
Number of Residues	4
Details	binding site for residue ZN C 1005

Chain	Residue
C	CYS334
C	CYS339
C	CYS354
C	CYS356

---

site_id	AD6
Number of Residues	4
Details	binding site for residue ZN C 1006

Chain	Residue
C	CYS361
C	CYS364
C	HIS369
C	CYS373

---

site_id	AD7
Number of Residues	4
Details	binding site for residue ZN C 1007

Chain	Residue
C	CYS415
C	CYS418
C	CYS433
C	CYS438

---

site_id	AD8
Number of Residues	4
Details	binding site for residue ZN C 1008

Chain	Residue
C	CYS443
C	CYS446
C	CYS454
C	HIS458

---

site_id	AD9
Number of Residues	3
Details	binding site for residue SO4 C 1009

Chain	Residue
C	TRP184
C	LYS232
C	ARG258

---

site_id	AE1
Number of Residues	8
Details	binding site for residue SO4 C 1010

Chain	Residue
A	HIS441
A	PRO449
C	GLY195
C	VAL196
C	CYS197
C	CYS202
C	GLU203
C	GLY204

---

site_id	AE2
Number of Residues	2
Details	binding site for residue SO4 C 1011

Chain	Residue
C	THR310
C	ASP311

---

site_id	AE3
Number of Residues	3
Details	binding site for residue SO4 D 101

Chain	Residue
D	ARG42
D	ARG72
D	ARG74

---

site_id	AE4
Number of Residues	4
Details	binding site for Di-peptide GLY D 75 and 3CN D 76

Chain	Residue
C	ASP346
C	CYS349
C	ARG351
D	ARG74

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
B	LYS27-ASP52

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	164
Details	Zinc finger: {"description":"RING-type 0; atypical","evidences":[{"source":"UniProtKB","id":"O60260","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	110
Details	Zinc finger: {"description":"RING-type 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU01221","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	116
Details	Zinc finger: {"description":"IBR-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU01221","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	82
Details	Zinc finger: {"description":"IBR-type","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	62
Details	Zinc finger: {"description":"RING-type 2; atypical","evidences":[{"source":"PROSITE-ProRule","id":"PRU01221","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	Active site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01221","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	24
Details	Binding site: {"evidences":[{"source":"PubMed","id":"26161729","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5CAW","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	40
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01221","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"26161729","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5CAW","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI9
Number of Residues	6
Details	Site: {"description":"Implicated in binding to phosphorylated ubiquitin","evidences":[{"source":"PubMed","id":"26161729","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI10
Number of Residues	2
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q7KTX7","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---