2VL2

Oxidized and reduced forms of human peroxiredoxin 5

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0008379	molecular_function	thioredoxin peroxidase activity
A	0016491	molecular_function	oxidoreductase activity
A	0034599	biological_process	cellular response to oxidative stress
B	0008379	molecular_function	thioredoxin peroxidase activity
B	0016491	molecular_function	oxidoreductase activity
B	0034599	biological_process	cellular response to oxidative stress
C	0008379	molecular_function	thioredoxin peroxidase activity
C	0016491	molecular_function	oxidoreductase activity
C	0034599	biological_process	cellular response to oxidative stress

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE BEZ A1162

Chain	Residue
A	THR44
A	PRO45
A	GLY46
A	CYS47
A	THR147
A	HOH2129
C	ALA64

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site_id	AC2
Number of Residues	11
Details	BINDING SITE FOR RESIDUE BEZ B1162

Chain	Residue
A	GLY66
B	PRO40
B	THR44
B	PRO45
B	GLY46
B	LEU116
B	PHE120
B	THR147
B	HOH2125
A	LYS63
A	ALA64

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Cysteine sulfenic acid (-SOH) intermediate => ECO:0000305|PubMed:10751410, ECO:0000305|PubMed:20643143

Chain	Residue	Details
C	ASP99
B	ASP99

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site_id	SWS_FT_FI2
Number of Residues	1
Details	MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P99029

Chain	Residue	Details
C	SER74
B	SER74

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site_id	SWS_FT_FI3
Number of Residues	1
Details	MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P99029

Chain	Residue	Details
C	GLY82
B	GLY82

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site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P99029

Chain	Residue	Details
C	SER115
B	SER115

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site_id	SWS_FT_FI5
Number of Residues	1
Details	LIPID: S-palmitoyl cysteine => ECO:0000269|PubMed:31740833

Chain	Residue	Details
C	ASP99
B	ASP99

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