8YD3

Crystal structure of human Cu-Zn Superoxide Dismutase 1 in complex with 1,2,10-Decanetriol

This is a non-PDB format compatible entry.

Functional Information from PROSITE/UniProt

site_id	PS00087
Number of Residues	11
Details	SOD_CU_ZN_1 Copper/Zinc superoxide dismutase signature 1. GFHVHEfGDnT

Chain	Residue	Details
A	GLY44-THR54

---

site_id	PS00332
Number of Residues	12
Details	SOD_CU_ZN_2 Copper/Zinc superoxide dismutase signature 2. GNAGsRlACgvI

Chain	Residue	Details
A	GLY138-ILE149

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	30
Details	BINDING: BINDING => ECO:0000269|PubMed:12963370, ECO:0000269|PubMed:17548825

Chain	Residue	Details
A	HIS46
D	HIS46
D	HIS48
D	HIS120
E	HIS46
E	HIS48
E	HIS120
F	HIS46
F	HIS48
F	HIS120
G	HIS46
A	HIS48
G	HIS48
G	HIS120
H	HIS46
H	HIS48
H	HIS120
I	HIS46
I	HIS48
I	HIS120
J	HIS46
J	HIS48
A	HIS120
J	HIS120
B	HIS46
B	HIS48
B	HIS120
C	HIS46
C	HIS48
C	HIS120

---

site_id	SWS_FT_FI2
Number of Residues	40
Details	BINDING: BINDING => ECO:0000269|PubMed:20727846

Chain	Residue	Details
A	HIS63
C	HIS71
C	HIS80
C	ASP83
D	HIS63
D	HIS71
D	HIS80
D	ASP83
E	HIS63
E	HIS71
E	HIS80
A	HIS71
E	ASP83
F	HIS63
F	HIS71
F	HIS80
F	ASP83
G	HIS63
G	HIS71
G	HIS80
G	ASP83
H	HIS63
A	HIS80
H	HIS71
H	HIS80
H	ASP83
I	HIS63
I	HIS71
I	HIS80
I	ASP83
J	HIS63
J	HIS71
J	HIS80
A	ASP83
J	ASP83
B	HIS63
B	HIS71
B	HIS80
B	ASP83
C	HIS63

---

site_id	SWS_FT_FI3
Number of Residues	10
Details	MOD_RES: N-acetylalanine => ECO:0000269|PubMed:1463506, ECO:0000269|PubMed:7002610, ECO:0007744|PubMed:25944712

Chain	Residue	Details
A	ALA1
J	ALA1
B	ALA1
C	ALA1
D	ALA1
E	ALA1
F	ALA1
G	ALA1
H	ALA1
I	ALA1

---

site_id	SWS_FT_FI4
Number of Residues	30
Details	MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P08228

Chain	Residue	Details
A	LYS3
D	LYS3
D	LYS9
D	LYS91
E	LYS3
E	LYS9
E	LYS91
F	LYS3
F	LYS9
F	LYS91
G	LYS3
A	LYS9
G	LYS9
G	LYS91
H	LYS3
H	LYS9
H	LYS91
I	LYS3
I	LYS9
I	LYS91
J	LYS3
J	LYS9
A	LYS91
J	LYS91
B	LYS3
B	LYS9
B	LYS91
C	LYS3
C	LYS9
C	LYS91

---

site_id	SWS_FT_FI5
Number of Residues	10
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569

Chain	Residue	Details
A	SER98
J	SER98
B	SER98
C	SER98
D	SER98
E	SER98
F	SER98
G	SER98
H	SER98
I	SER98

---

site_id	SWS_FT_FI6
Number of Residues	10
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569

Chain	Residue	Details
A	SER102
J	SER102
B	SER102
C	SER102
D	SER102
E	SER102
F	SER102
G	SER102
H	SER102
I	SER102

---

site_id	SWS_FT_FI7
Number of Residues	10
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P07632

Chain	Residue	Details
A	SER105
J	SER105
B	SER105
C	SER105
D	SER105
E	SER105
F	SER105
G	SER105
H	SER105
I	SER105

---

site_id	SWS_FT_FI8
Number of Residues	10
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P08228

Chain	Residue	Details
A	SER107
J	SER107
B	SER107
C	SER107
D	SER107
E	SER107
F	SER107
G	SER107
H	SER107
I	SER107

---

site_id	SWS_FT_FI9
Number of Residues	10
Details	MOD_RES: N6-succinyllysine; alternate => ECO:0000269|PubMed:24140062

Chain	Residue	Details
A	LYS122
J	LYS122
B	LYS122
C	LYS122
D	LYS122
E	LYS122
F	LYS122
G	LYS122
H	LYS122
I	LYS122

---

site_id	SWS_FT_FI10
Number of Residues	10
Details	MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P08228

Chain	Residue	Details
A	LYS136
J	LYS136
B	LYS136
C	LYS136
D	LYS136
E	LYS136
F	LYS136
G	LYS136
H	LYS136
I	LYS136

---

site_id	SWS_FT_FI11
Number of Residues	10
Details	LIPID: S-palmitoyl cysteine => ECO:0000269|PubMed:22496122

Chain	Residue	Details
A	CYS6
J	CYS6
B	CYS6
C	CYS6
D	CYS6
E	CYS6
F	CYS6
G	CYS6
H	CYS6
I	CYS6

---

site_id	SWS_FT_FI12
Number of Residues	20
Details	CROSSLNK: 1-(tryptophan-3-yl)-tryptophan (Trp-Trp) (interchain with W-33) => ECO:0000269|PubMed:20600836

Chain	Residue	Details
A	TRP32
F	TRP32
G	TRP32
H	TRP32
I	TRP32
J	TRP32
B	TRP32
C	TRP32
D	TRP32
E	TRP32

---