3H7S

Crystal structures of K63-linked di- and tri-ubiquitin reveal a highly extended chain architecture

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 101

Chain	Residue
A	MET1
A	GLU16
A	ASP32
A	HOH220

---

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 102

Chain	Residue
A	GLU18
A	ASP21
A	HOH201
A	HOH203

---

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 103

Chain	Residue
A	ASP52
A	HOH208
A	HOH216
A	GLU24

---

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ZN A 104

Chain	Residue
A	LYS6
A	GLU64
A	HIS68
A	HOH205
A	HOH206
A	HOH217

---

site_id	AC5
Number of Residues	1
Details	BINDING SITE FOR RESIDUE ZN A 105

Chain	Residue
B	HIS68

---

site_id	AC6
Number of Residues	1
Details	BINDING SITE FOR RESIDUE ZN A 106

Chain	Residue
B	ZN104

---

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN B 101

Chain	Residue
B	GLU18
B	ASP21
B	HOH201
B	HOH223

---

site_id	AC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE ZN B 102

Chain	Residue
B	GLU24
B	ASP52
B	HOH214

---

site_id	AC9
Number of Residues	2
Details	BINDING SITE FOR RESIDUE ZN B 103

Chain	Residue
B	GLU64
B	HIS68

---

site_id	BC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN B 104

Chain	Residue
A	ZN106
B	MET1
B	GLU16
B	ASP32

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	LYS27-ASP52

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	SITE: Interacts with activating enzyme

Chain	Residue	Details
A	ARG54
A	ARG72
B	ARG54
B	ARG72

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	SITE: Essential for function

Chain	Residue	Details
A	HIS68
B	HIS68

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	MOD_RES: Phosphoserine; by PINK1 => ECO:0000269|PubMed:24660806, ECO:0000269|PubMed:24751536, ECO:0000269|PubMed:24784582, ECO:0000269|PubMed:25527291

Chain	Residue	Details
A	SER65
B	SER65

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	MOD_RES: (Microbial infection) ADP-ribosylthreonine => ECO:0000269|PubMed:32330457

Chain	Residue	Details
A	THR66
B	THR66

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	MOD_RES: ADP-ribosylglycine => ECO:0000269|PubMed:28525742

Chain	Residue	Details
A	GLY76
B	GLY76

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603

Chain	Residue	Details
A	LYS6
B	LYS6

---

site_id	SWS_FT_FI7
Number of Residues	4
Details	CROSSLNK: Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)

Chain	Residue	Details
A	GLY76
B	GLY76

---

site_id	SWS_FT_FI8
Number of Residues	4
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603, ECO:0000269|PubMed:16543144

Chain	Residue	Details
A	LYS11
A	LYS48
B	LYS11
B	LYS48

---

site_id	SWS_FT_FI9
Number of Residues	2
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000305|PubMed:15466860

Chain	Residue	Details
A	LYS27
B	LYS27

---

site_id	SWS_FT_FI10
Number of Residues	2
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:25752573, ECO:0000269|PubMed:25752577, ECO:0000269|PubMed:34239127

Chain	Residue	Details
A	LYS29
B	LYS29

---

site_id	SWS_FT_FI11
Number of Residues	2
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:25752577

Chain	Residue	Details
A	LYS33
B	LYS33

---

site_id	SWS_FT_FI12
Number of Residues	2
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:18719106

Chain	Residue	Details
A	ARG63
B	ARG63

---