2Z5Z
Crystal structure of the complex of buffalo Lactoperoxidase with fluoride ion at 3.5A resolution
Functional Information from GO Data
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:P05164, ECO:0000255|PROSITE-ProRule:PRU00298 |
Chain | Residue | Details |
A | HIS109 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | BINDING: covalent => ECO:0000269|PubMed:19339248, ECO:0000269|Ref.5, ECO:0000269|Ref.6 |
Chain | Residue | Details |
A | ASP108 | |
A | GLU258 |
site_id | SWS_FT_FI3 |
Number of Residues | 5 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00298, ECO:0000269|PubMed:19339248, ECO:0000269|Ref.5, ECO:0000269|Ref.6 |
Chain | Residue | Details |
A | ASP110 | |
A | THR184 | |
A | PHE186 | |
A | ASP188 | |
A | SER190 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | BINDING: axial binding residue => ECO:0000269|PubMed:19339248 |
Chain | Residue | Details |
A | HIS351 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | SITE: Transition state stabilizer => ECO:0000250|UniProtKB:P05164, ECO:0000255|PROSITE-ProRule:PRU00298 |
Chain | Residue | Details |
A | ARG255 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:19339248, ECO:0000269|Ref.6 |
Chain | Residue | Details |
A | SEP198 |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | MOD_RES: 3'-nitrotyrosine => ECO:0000250|UniProtKB:P11678 |
Chain | Residue | Details |
A | TYR365 |
site_id | SWS_FT_FI8 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) (high mannose) asparagine; alternate => ECO:0000269|PubMed:19339248, ECO:0000269|PubMed:30296068, ECO:0000269|Ref.5, ECO:0000269|Ref.6 |
Chain | Residue | Details |
A | ASN95 |
site_id | SWS_FT_FI9 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) (high mannose) asparagine => ECO:0000269|PubMed:19339248, ECO:0000269|PubMed:30296068, ECO:0000269|Ref.5, ECO:0000269|Ref.6 |
Chain | Residue | Details |
A | ASN205 |
site_id | SWS_FT_FI10 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19339248, ECO:0000269|Ref.5, ECO:0000269|Ref.6 |
Chain | Residue | Details |
A | ASN241 |
site_id | SWS_FT_FI11 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) (hybrid) asparagine; alternate => ECO:0000269|PubMed:19339248, ECO:0000269|PubMed:30296068, ECO:0000269|Ref.5, ECO:0000269|Ref.6 |
Chain | Residue | Details |
A | ASN332 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1mhl |
Chain | Residue | Details |
A | HIS109 | |
A | GLN105 |
site_id | CSA2 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1mhl |
Chain | Residue | Details |
A | ARG255 |
site_id | MCSA1 |
Number of Residues | 9 |
Details | M-CSA 944 |
Chain | Residue | Details |
A | GLN105 | transition state stabiliser |
A | ASP108 | alter redox potential, covalently attached |
A | ASP110 | metal ligand |
A | THR184 | metal ligand |
A | PHE186 | metal ligand |
A | ASP188 | metal ligand |
A | SER190 | metal ligand |
A | GLU258 | alter redox potential, covalently attached |
A | HIS351 | metal ligand |