3FAQ
Crystal structure of lactoperoxidase complex with cyanide
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 | THR184 | |
| A | PHE186 | |
| A | ASP188 | |
| A | SER190 | |
| A | ASP110 |
| 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 | 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 |
