6WI8

Inhibitor compound-induced confrontational change in Ring1b-Bmi1 domain structure

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	binding site for residue ZN A 1201

Chain	Residue
A	ARG26
A	CYS1018
A	CYS1021
A	CYS1039
A	CYS1042

---

site_id	AC2
Number of Residues	4
Details	binding site for residue ZN A 1202

Chain	Residue
A	CYS1034
A	HIS1036
A	CYS1053
A	CYS1056

---

site_id	AC3
Number of Residues	4
Details	binding site for residue ZN A 1203

Chain	Residue
A	CYS67
A	HIS69
A	CYS87
A	CYS90

---

site_id	AC4
Number of Residues	4
Details	binding site for residue ZN A 1204

Chain	Residue
A	CYS51
A	CYS54
A	CYS72
A	CYS75

---

site_id	AC5
Number of Residues	4
Details	binding site for residue ZN B 1201

Chain	Residue
B	CYS1018
B	CYS1021
B	CYS1039
B	CYS1042

---

site_id	AC6
Number of Residues	4
Details	binding site for residue ZN B 1202

Chain	Residue
B	CYS1034
B	HIS1036
B	CYS1053
B	CYS1056

---

site_id	AC7
Number of Residues	4
Details	binding site for residue ZN B 1203

Chain	Residue
B	CYS67
B	HIS69
B	CYS87
B	CYS90

---

site_id	AC8
Number of Residues	4
Details	binding site for residue ZN B 1204

Chain	Residue
B	CYS51
B	CYS54
B	CYS72
B	CYS75

---

Functional Information from PROSITE/UniProt

site_id	PS00518
Number of Residues	10
Details	ZF_RING_1 Zinc finger RING-type signature. ClHrFCadCI

Chain	Residue	Details
A	CYS67-ILE76
A	CYS1034-ILE1043

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	158
Details	ZN_FING: RING-type => ECO:0000255|PROSITE-ProRule:PRU00175

Chain	Residue	Details
A	CYS1018-ASP1057
B	CYS1018-ASP1057
A	CYS51-ARG91
B	CYS51-ARG91

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0000269|PubMed:25519132

Chain	Residue	Details
A	SER41
B	SER41

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:Q9CQJ4

Chain	Residue	Details
A	LYS112
B	LYS112

---