Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3GTV

Human-mouse SOD1 chimera

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005507	molecular_function	copper ion binding
A	0006801	biological_process	superoxide metabolic process
A	0046872	molecular_function	metal ion binding
B	0005507	molecular_function	copper ion binding
B	0006801	biological_process	superoxide metabolic process
B	0046872	molecular_function	metal ion binding
C	0005507	molecular_function	copper ion binding
C	0006801	biological_process	superoxide metabolic process
C	0046872	molecular_function	metal ion binding
D	0005507	molecular_function	copper ion binding
D	0006801	biological_process	superoxide metabolic process
D	0046872	molecular_function	metal ion binding
E	0005507	molecular_function	copper ion binding
E	0006801	biological_process	superoxide metabolic process
E	0046872	molecular_function	metal ion binding
F	0005507	molecular_function	copper ion binding
F	0006801	biological_process	superoxide metabolic process
F	0046872	molecular_function	metal ion binding
G	0005507	molecular_function	copper ion binding
G	0006801	biological_process	superoxide metabolic process
G	0046872	molecular_function	metal ion binding
H	0005507	molecular_function	copper ion binding
H	0006801	biological_process	superoxide metabolic process
H	0046872	molecular_function	metal ion binding
I	0005507	molecular_function	copper ion binding
I	0006801	biological_process	superoxide metabolic process
I	0046872	molecular_function	metal ion binding
J	0005507	molecular_function	copper ion binding
J	0006801	biological_process	superoxide metabolic process
J	0046872	molecular_function	metal ion binding
K	0005507	molecular_function	copper ion binding
K	0006801	biological_process	superoxide metabolic process
K	0046872	molecular_function	metal ion binding
L	0005507	molecular_function	copper ion binding
L	0006801	biological_process	superoxide metabolic process
L	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 155

Chain	Residue
A	HIS63
A	HIS71
A	HIS80
A	ASP83

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN B 155

Chain	Residue
B	HIS63
B	HIS71
B	HIS80
B	ASP83

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN C 155

Chain	Residue
C	HIS71
C	HIS80
C	ASP83
C	HIS63

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN D 155

Chain	Residue
D	HIS63
D	HIS71
D	HIS80
D	ASP83

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN E 155

Chain	Residue
E	HIS63
E	HIS71
E	HIS80
E	ASP83
E	LYS136

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN F 155

Chain	Residue
F	HIS63
F	HIS71
F	HIS80
F	ASP83
F	LYS136

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN G 155

Chain	Residue
G	HIS63
G	HIS71
G	HIS80
G	ASP83

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN H 155

Chain	Residue
H	HIS63
H	HIS71
H	HIS80
H	ASP83

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN I 155

Chain	Residue
I	HIS63
I	HIS71
I	HIS80
I	ASP83

site_id	BC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN J 155

Chain	Residue
J	HIS63
J	HIS71
J	HIS80
J	ASP83

site_id	BC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN K 155

Chain	Residue
K	HIS63
K	HIS71
K	HIS80
K	ASP83

site_id	BC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN L 155

Chain	Residue
L	HIS63
L	HIS71
L	HIS80
L	ASP83

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	36
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	48
Details	Binding site: {"evidences":[{"source":"PubMed","id":"20727846","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	12
Details	Modified residue: {"description":"N-acetylalanine","evidences":[{"source":"PubMed","id":"23806337","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	36
Details	Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"PubMed","id":"23806337","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	12
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P00441","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	12
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	12
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P07632","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	12
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"21183079","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	24
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"PubMed","id":"23806337","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	12
Details	Lipidation: {"description":"S-palmitoyl cysteine","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	24
Details	Cross-link: {"description":"1-(tryptophan-3-yl)-tryptophan (Trp-Trp) (interchain with W-33)","evidences":[{"source":"PubMed","id":"20600836","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)