1VKM
Crystal structure of an indigoidine synthase a (idga)-like protein (tm1464) from thermotoga maritima msb8 at 1.90 A resolution
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0001522 | biological_process | pseudouridine synthesis |
| A | 0004730 | molecular_function | pseudouridylate synthase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| A | 0016829 | molecular_function | lyase activity |
| A | 0046113 | biological_process | nucleobase catabolic process |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0001522 | biological_process | pseudouridine synthesis |
| B | 0004730 | molecular_function | pseudouridylate synthase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| B | 0016829 | molecular_function | lyase activity |
| B | 0046113 | biological_process | nucleobase catabolic process |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0001522 | biological_process | pseudouridine synthesis |
| C | 0004730 | molecular_function | pseudouridylate synthase activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| C | 0016829 | molecular_function | lyase activity |
| C | 0046113 | biological_process | nucleobase catabolic process |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0001522 | biological_process | pseudouridine synthesis |
| D | 0004730 | molecular_function | pseudouridylate synthase activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| D | 0016829 | molecular_function | lyase activity |
| D | 0046113 | biological_process | nucleobase catabolic process |
| D | 0046872 | molecular_function | metal ion binding |
| E | 0001522 | biological_process | pseudouridine synthesis |
| E | 0004730 | molecular_function | pseudouridylate synthase activity |
| E | 0005737 | cellular_component | cytoplasm |
| E | 0016787 | molecular_function | hydrolase activity |
| E | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| E | 0016829 | molecular_function | lyase activity |
| E | 0046113 | biological_process | nucleobase catabolic process |
| E | 0046872 | molecular_function | metal ion binding |
| F | 0001522 | biological_process | pseudouridine synthesis |
| F | 0004730 | molecular_function | pseudouridylate synthase activity |
| F | 0005737 | cellular_component | cytoplasm |
| F | 0016787 | molecular_function | hydrolase activity |
| F | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| F | 0016829 | molecular_function | lyase activity |
| F | 0046113 | biological_process | nucleobase catabolic process |
| F | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN A 300 |
| Chain | Residue |
| A | HIS-4 |
| A | HIS-2 |
| C | GLU204 |
| C | GLU206 |
| C | HOH612 |
| E | HIS-5 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN A 400 |
| Chain | Residue |
| A | HOH606 |
| A | HOH611 |
| C | HOH604 |
| A | ASP126 |
| A | HOH602 |
| A | HOH605 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN B 300 |
| Chain | Residue |
| A | GLU204 |
| A | GLU206 |
| A | HOH626 |
| B | HIS-2 |
| B | HIS-4 |
| F | HIS-5 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN B 400 |
| Chain | Residue |
| A | HOH616 |
| A | HOH636 |
| B | ASP126 |
| B | HOH604 |
| B | HOH607 |
| B | HOH609 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN C 300 |
| Chain | Residue |
| B | GLU204 |
| B | GLU206 |
| B | HOH614 |
| C | HIS-2 |
| C | HIS-4 |
| D | HIS-5 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN C 400 |
| Chain | Residue |
| B | HOH613 |
| C | ASP126 |
| C | HOH610 |
| C | HOH614 |
| C | HOH621 |
| C | HOH636 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN D 300 |
| Chain | Residue |
| C | HIS-5 |
| D | HIS-2 |
| D | HIS-4 |
| E | GLU204 |
| E | GLU206 |
| E | HOH618 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN D 400 |
| Chain | Residue |
| D | ASP126 |
| D | HOH603 |
| D | HOH605 |
| D | HOH609 |
| E | HOH604 |
| E | HOH606 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN E 300 |
| Chain | Residue |
| A | HIS-5 |
| E | HIS-2 |
| E | HIS-4 |
| F | GLU204 |
| F | GLU206 |
| F | HOH605 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN E 400 |
| Chain | Residue |
| E | ASP126 |
| E | HOH609 |
| E | HOH611 |
| E | HOH619 |
| F | HOH618 |
| F | HOH623 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN F 300 |
| Chain | Residue |
| B | HIS-5 |
| D | GLU204 |
| D | GLU206 |
| D | HOH614 |
| F | HIS-2 |
| F | HIS-4 |
| site_id | BC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN F 400 |
| Chain | Residue |
| D | HOH606 |
| D | HOH607 |
| F | ASP126 |
| F | HOH601 |
| F | HOH602 |
| F | HOH603 |
| site_id | BC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN C 401 |
| Chain | Residue |
| C | GLU64 |
| C | GLU65 |
| C | GLU68 |
| C | HOH686 |
| C | HOH716 |
| C | HOH722 |
| site_id | BC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN A 401 |
| Chain | Residue |
| A | GLU229 |
| A | HOH808 |
| A | HOH811 |
| A | HOH818 |
| F | GLU220 |
| site_id | BC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MN F 401 |
| Chain | Residue |
| C | GLU4 |
| F | GLU229 |
| F | GLU233 |
| F | HOH736 |
| F | HOH745 |
| F | HOH748 |
| F | HOH755 |
| site_id | BC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MN E 401 |
| Chain | Residue |
| D | HOH760 |
| E | HOH717 |
| site_id | BC8 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE UNL A 600 |
| Chain | Residue |
| A | SER128 |
| A | ASP130 |
| A | LYS147 |
| A | HOH603 |
| A | HOH606 |
| A | HOH608 |
| A | HOH610 |
| A | HOH611 |
| A | HOH612 |
| A | HOH644 |
| A | HOH662 |
| A | HOH790 |
| A | GLU17 |
| A | THR19 |
| A | LYS77 |
| A | THR96 |
| A | VAL97 |
| A | THR114 |
| A | GLY116 |
| site_id | BC9 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE UNL B 600 |
| Chain | Residue |
| A | HOH616 |
| B | GLU17 |
| B | THR19 |
| B | LYS77 |
| B | THR96 |
| B | VAL97 |
| B | THR114 |
| B | GLY116 |
| B | SER128 |
| B | ASP130 |
| B | LYS147 |
| B | THR245 |
| B | EDO601 |
| B | HOH605 |
| B | HOH609 |
| B | HOH610 |
| B | HOH625 |
| B | HOH642 |
| B | HOH644 |
| site_id | CC1 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE UNL C 600 |
| Chain | Residue |
| C | GLU17 |
| C | THR19 |
| C | LYS77 |
| C | THR96 |
| C | VAL97 |
| C | THR114 |
| C | GLY116 |
| C | SER128 |
| C | ASP130 |
| C | LYS147 |
| C | HOH605 |
| C | HOH614 |
| C | HOH629 |
| C | HOH632 |
| C | HOH636 |
| C | HOH643 |
| C | HOH646 |
| C | HOH654 |
| C | HOH736 |
| site_id | CC2 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE UNL D 600 |
| Chain | Residue |
| D | GLU17 |
| D | THR19 |
| D | LYS77 |
| D | THR96 |
| D | VAL97 |
| D | THR114 |
| D | GLY116 |
| D | SER128 |
| D | ASP130 |
| D | LYS147 |
| D | THR245 |
| D | HOH608 |
| D | HOH609 |
| D | HOH612 |
| D | HOH621 |
| D | HOH633 |
| D | HOH644 |
| D | HOH659 |
| D | HOH744 |
| E | HOH604 |
| site_id | CC3 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE UNL E 600 |
| Chain | Residue |
| E | GLU17 |
| E | THR19 |
| E | LYS77 |
| E | THR96 |
| E | VAL97 |
| E | THR114 |
| E | GLY116 |
| E | SER128 |
| E | ASP130 |
| E | LYS147 |
| E | HOH608 |
| E | HOH611 |
| E | HOH616 |
| E | HOH652 |
| E | HOH678 |
| E | HOH693 |
| E | HOH700 |
| F | HOH618 |
| site_id | CC4 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE UNL F 600 |
| Chain | Residue |
| D | HOH607 |
| F | GLU17 |
| F | THR19 |
| F | LYS77 |
| F | THR96 |
| F | VAL97 |
| F | THR114 |
| F | GLY116 |
| F | SER128 |
| F | ASP130 |
| F | LYS147 |
| F | HOH602 |
| F | HOH604 |
| F | HOH608 |
| F | HOH610 |
| F | HOH626 |
| F | HOH644 |
| F | HOH659 |
| site_id | CC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO D 601 |
| Chain | Residue |
| D | ARG81 |
| D | HOH624 |
| D | HOH632 |
| E | LEU166 |
| E | PRO187 |
| site_id | CC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO C 601 |
| Chain | Residue |
| C | HIS-2 |
| C | HIS-5 |
| D | HIS-2 |
| D | HIS-5 |
| site_id | CC7 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE EDO B 601 |
| Chain | Residue |
| B | GLU17 |
| B | VAL20 |
| B | THR114 |
| B | GLY115 |
| B | GLY116 |
| B | LYS147 |
| B | PHE177 |
| B | ASN264 |
| B | UNL600 |
| B | HOH697 |
| site_id | CC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO E 601 |
| Chain | Residue |
| E | THR132 |
| E | SER135 |
| E | HOH708 |
| E | HOH710 |
| F | LEU162 |
| site_id | CC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO B 602 |
| Chain | Residue |
| B | PRO165 |
| B | LEU166 |
| B | HOH627 |
| B | HOH664 |
| C | ARG81 |
| site_id | DC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 601 |
| Chain | Residue |
| A | HIS-5 |
| A | HIS-2 |
| A | HIS-4 |
| E | HIS-2 |
| site_id | DC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO D 602 |
| Chain | Residue |
| D | ASP76 |
| D | VAL78 |
| D | ILE85 |
| D | VAL86 |
| D | HOH657 |
| E | ARG185 |
| site_id | DC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO E 602 |
| Chain | Residue |
| D | VAL127 |
| E | MSE158 |
| E | HOH610 |
| E | HOH637 |
| site_id | DC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO E 603 |
| Chain | Residue |
| E | LEU150 |
| E | ASP151 |
| E | VAL152 |
| E | GLU153 |
| E | HOH654 |
| E | HOH696 |
| E | HOH702 |
| site_id | DC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO C 602 |
| Chain | Residue |
| C | ARG138 |
| C | LYS203 |
| C | HOH730 |
| E | LYS-7 |
| site_id | DC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO B 603 |
| Chain | Residue |
| B | HIS-2 |
| B | HIS-5 |
| B | HOH663 |
| F | HIS-2 |
| F | HIS-3 |
| F | HIS-4 |
| F | HIS-5 |
| F | HOH704 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"HAMAP-Rule","id":"MF_01876","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"HAMAP-Rule","id":"MF_01876","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 24 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01876","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01876","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15822122","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1VKM","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |






