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4Y55

Crystal structure of Buffalo lactoperoxidase with Rhodanide at 2.09 Angstrom resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0004601molecular_functionperoxidase activity
A0006979biological_processresponse to oxidative stress
A0020037molecular_functionheme binding
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:P05164, ECO:0000255|PROSITE-ProRule:PRU00298
ChainResidueDetails
AHIS109

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: covalent => ECO:0000269|PubMed:19339248, ECO:0000269|Ref.5, ECO:0000269|Ref.6
ChainResidueDetails
AASP108
AGLU258

site_idSWS_FT_FI3
Number of Residues5
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00298, ECO:0000269|PubMed:19339248, ECO:0000269|Ref.5, ECO:0000269|Ref.6
ChainResidueDetails
AASP110
ATHR184
APHE186
AASP188
ASER190

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: axial binding residue => ECO:0000269|PubMed:19339248
ChainResidueDetails
AHIS351

site_idSWS_FT_FI5
Number of Residues1
DetailsSITE: Transition state stabilizer => ECO:0000250|UniProtKB:P05164, ECO:0000255|PROSITE-ProRule:PRU00298
ChainResidueDetails
AARG255

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:19339248, ECO:0000269|Ref.6
ChainResidueDetails
ASEP198

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: 3'-nitrotyrosine => ECO:0000250|UniProtKB:P11678
ChainResidueDetails
ATYR365

site_idSWS_FT_FI8
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) (high mannose) asparagine; alternate => ECO:0000269|PubMed:19339248, ECO:0000269|PubMed:30296068, ECO:0000269|Ref.5, ECO:0000269|Ref.6
ChainResidueDetails
AASN95

site_idSWS_FT_FI9
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) (high mannose) asparagine => ECO:0000269|PubMed:19339248, ECO:0000269|PubMed:30296068, ECO:0000269|Ref.5, ECO:0000269|Ref.6
ChainResidueDetails
AASN205

site_idSWS_FT_FI10
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19339248, ECO:0000269|Ref.5, ECO:0000269|Ref.6
ChainResidueDetails
AASN241

site_idSWS_FT_FI11
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) (hybrid) asparagine; alternate => ECO:0000269|PubMed:19339248, ECO:0000269|PubMed:30296068, ECO:0000269|Ref.5, ECO:0000269|Ref.6
ChainResidueDetails
AASN332

Catalytic Information from CSA
site_idMCSA1
Number of Residues9
DetailsM-CSA 944
ChainResidueDetails
AGLN105transition state stabiliser
AASP108alter redox potential, covalently attached
AASP110metal ligand
ATHR184metal ligand
APHE186metal ligand
AASP188metal ligand
ASER190metal ligand
AGLU258alter redox potential, covalently attached
AHIS351metal ligand

227344

PDB entries from 2024-11-13

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