1F18

Crystal structure of yeast copper-zinc superoxide dismutase mutant GLY85ARG

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004784	molecular_function	superoxide dismutase activity
A	0005507	molecular_function	copper ion binding
A	0005515	molecular_function	protein binding
A	0005634	cellular_component	nucleus
A	0005737	cellular_component	cytoplasm
A	0005739	cellular_component	mitochondrion
A	0005758	cellular_component	mitochondrial intermembrane space
A	0005777	cellular_component	peroxisome
A	0005829	cellular_component	cytosol
A	0006801	biological_process	superoxide metabolic process
A	0006878	biological_process	intracellular copper ion homeostasis
A	0006882	biological_process	intracellular zinc ion homeostasis
A	0008270	molecular_function	zinc ion binding
A	0015680	biological_process	protein maturation by copper ion transfer
A	0016209	molecular_function	antioxidant activity
A	0016491	molecular_function	oxidoreductase activity
A	0019430	biological_process	removal of superoxide radicals
A	0031505	biological_process	fungal-type cell wall organization
A	0034599	biological_process	cellular response to oxidative stress
A	0045944	biological_process	positive regulation of transcription by RNA polymerase II
A	0046872	molecular_function	metal ion binding
A	0050821	biological_process	protein stabilization
A	1901856	biological_process	negative regulation of cellular respiration
A	1902693	cellular_component	superoxide dismutase complex

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CU A 154

Chain	Residue
A	HIS46
A	HIS48
A	HIS63
A	HIS120

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

Chain	Residue
A	HIS63
A	HIS71
A	HIS80
A	ASP83

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Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	GLY44-THR54

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

Chain	Residue	Details
A	GLY138-ILE149

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	BINDING: in apo form => ECO:0000269|PubMed:10026301, ECO:0000269|PubMed:11524675

Chain	Residue	Details
A	ARG43

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site_id	SWS_FT_FI2
Number of Residues	3
Details	BINDING: BINDING => ECO:0000269|PubMed:10026301, ECO:0000269|PubMed:8652572

Chain	Residue	Details
A	ILE47
A	GLU49
A	ALA121

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|PubMed:10026301, ECO:0000269|PubMed:11524675

Chain	Residue	Details
A	PHE64
A	GLY72
A	VAL81
A	MET84

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	BINDING: BINDING => ECO:0000305

Chain	Residue	Details
A	PRO144

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site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:18407956

Chain	Residue	Details
A	GLU26

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site_id	SWS_FT_FI6
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:15665377, ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198

Chain	Residue	Details
A	PRO39

---

site_id	SWS_FT_FI7
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:17287358, ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198

Chain	Residue	Details
A	PHE99

---

site_id	SWS_FT_FI8
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:17287358

Chain	Residue	Details
A	VAL117

---

site_id	SWS_FT_FI9
Number of Residues	1
Details	MOD_RES: Phosphothreonine => ECO:0007744|PubMed:17287358

Chain	Residue	Details
A	GLU132

---

site_id	SWS_FT_FI10
Number of Residues	1
Details	MOD_RES: Phosphothreonine => ECO:0007744|PubMed:19779198

Chain	Residue	Details
A	GLY138

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site_id	SWS_FT_FI11
Number of Residues	3
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) => ECO:0000269|PubMed:15166219

Chain	Residue	Details
A	PHE19
A	THR70

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	8
Details	M-CSA 138

Chain	Residue	Details
A	ILE47	metal ligand
A	GLU49	metal ligand
A	PHE64	hydrogen bond acceptor, hydrogen bond donor, metal ligand, proton acceptor, proton donor
A	GLY72	metal ligand
A	VAL81	metal ligand
A	MET84	metal ligand
A	ALA121	metal ligand
A	PRO144	electrostatic stabiliser, hydrogen bond donor

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