2BRY
Crystal structure of the native monooxygenase domain of MICAL at 1.45 A resolution
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL A1490 |
| Chain | Residue |
| A | CYS23 |
| A | LYS118 |
| A | PHE119 |
| A | ARG158 |
| A | HOH2271 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SO4 A1492 |
| Chain | Residue |
| A | HOH2745 |
| A | HOH2746 |
| A | HOH2747 |
| A | HOH2749 |
| A | HOH2750 |
| A | LYS86 |
| A | ARG109 |
| A | GLN205 |
| A | TYR209 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL B1490 |
| Chain | Residue |
| B | CYS23 |
| B | LYS118 |
| B | PHE119 |
| B | ARG158 |
| B | HOH2104 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 B1491 |
| Chain | Residue |
| B | HIS176 |
| B | TRP177 |
| B | HOH2396 |
| B | HOH2815 |
| B | HOH2816 |
| B | HOH2817 |
| B | HOH2818 |
| B | HOH2819 |
| site_id | AC5 |
| Number of Residues | 33 |
| Details | BINDING SITE FOR RESIDUE FAD A1493 |
| Chain | Residue |
| A | VAL90 |
| A | GLY91 |
| A | GLY93 |
| A | PRO94 |
| A | CYS95 |
| A | VAL113 |
| A | GLU114 |
| A | LYS115 |
| A | ARG116 |
| A | ARG121 |
| A | ASN123 |
| A | LEU125 |
| A | ILE157 |
| A | VAL179 |
| A | LYS180 |
| A | PHE181 |
| A | ALA217 |
| A | ALA218 |
| A | GLY219 |
| A | THR241 |
| A | TYR293 |
| A | GLY392 |
| A | ASP393 |
| A | TRP400 |
| A | HOH2258 |
| A | HOH2510 |
| A | HOH2619 |
| A | HOH2752 |
| A | HOH2753 |
| A | HOH2754 |
| A | HOH2755 |
| A | HOH2756 |
| A | HOH2757 |
| site_id | AC6 |
| Number of Residues | 34 |
| Details | BINDING SITE FOR RESIDUE FAD B1492 |
| Chain | Residue |
| B | VAL90 |
| B | GLY91 |
| B | GLY93 |
| B | PRO94 |
| B | CYS95 |
| B | GLU114 |
| B | LYS115 |
| B | ARG116 |
| B | ARG121 |
| B | ASN123 |
| B | VAL124 |
| B | LEU125 |
| B | ILE157 |
| B | VAL179 |
| B | LYS180 |
| B | PHE181 |
| B | ALA217 |
| B | ALA218 |
| B | GLY219 |
| B | THR241 |
| B | TYR293 |
| B | GLY392 |
| B | ASP393 |
| B | TRP400 |
| B | HOH2453 |
| B | HOH2555 |
| B | HOH2686 |
| B | HOH2705 |
| B | HOH2820 |
| B | HOH2821 |
| B | HOH2822 |
| B | HOH2823 |
| B | HOH2824 |
| B | HOH2825 |
| site_id | AC7 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL A1491 |
| Chain | Residue |
| A | HOH2743 |
| A | HOH2744 |
| B | ARG146 |
| B | ARG248 |
| B | THR253 |
| A | ARG146 |
| A | ARG248 |
| A | THR253 |
| A | HOH2233 |
| A | HOH2742 |
Functional Information from PROSITE/UniProt
| site_id | PS00070 |
| Number of Residues | 12 |
| Details | ALDEHYDE_DEHYDR_CYS Aldehyde dehydrogenases cysteine active site. VyQQGQACTNTK |
| Chain | Residue | Details |
| A | VAL75-LYS86 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 16 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"16275925","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4TXI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4TXK","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"D3ZBP4","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
