1EQ2
THE CRYSTAL STRUCTURE OF ADP-L-GLYCERO-D-MANNOHEPTOSE 6-EPIMERASE
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005515 | molecular_function | protein binding |
| A | 0005829 | cellular_component | cytosol |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0008712 | molecular_function | ADP-glyceromanno-heptose 6-epimerase activity |
| A | 0009103 | biological_process | lipopolysaccharide biosynthetic process |
| A | 0009244 | biological_process | lipopolysaccharide core region biosynthetic process |
| A | 0016020 | cellular_component | membrane |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0050661 | molecular_function | NADP binding |
| A | 0070401 | molecular_function | NADP+ binding |
| A | 0097171 | biological_process | ADP-L-glycero-beta-D-manno-heptose biosynthetic process |
| B | 0005515 | molecular_function | protein binding |
| B | 0005829 | cellular_component | cytosol |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0008712 | molecular_function | ADP-glyceromanno-heptose 6-epimerase activity |
| B | 0009103 | biological_process | lipopolysaccharide biosynthetic process |
| B | 0009244 | biological_process | lipopolysaccharide core region biosynthetic process |
| B | 0016020 | cellular_component | membrane |
| B | 0016853 | molecular_function | isomerase activity |
| B | 0050661 | molecular_function | NADP binding |
| B | 0070401 | molecular_function | NADP+ binding |
| B | 0097171 | biological_process | ADP-L-glycero-beta-D-manno-heptose biosynthetic process |
| C | 0005515 | molecular_function | protein binding |
| C | 0005829 | cellular_component | cytosol |
| C | 0005975 | biological_process | carbohydrate metabolic process |
| C | 0008712 | molecular_function | ADP-glyceromanno-heptose 6-epimerase activity |
| C | 0009103 | biological_process | lipopolysaccharide biosynthetic process |
| C | 0009244 | biological_process | lipopolysaccharide core region biosynthetic process |
| C | 0016020 | cellular_component | membrane |
| C | 0016853 | molecular_function | isomerase activity |
| C | 0050661 | molecular_function | NADP binding |
| C | 0070401 | molecular_function | NADP+ binding |
| C | 0097171 | biological_process | ADP-L-glycero-beta-D-manno-heptose biosynthetic process |
| D | 0005515 | molecular_function | protein binding |
| D | 0005829 | cellular_component | cytosol |
| D | 0005975 | biological_process | carbohydrate metabolic process |
| D | 0008712 | molecular_function | ADP-glyceromanno-heptose 6-epimerase activity |
| D | 0009103 | biological_process | lipopolysaccharide biosynthetic process |
| D | 0009244 | biological_process | lipopolysaccharide core region biosynthetic process |
| D | 0016020 | cellular_component | membrane |
| D | 0016853 | molecular_function | isomerase activity |
| D | 0050661 | molecular_function | NADP binding |
| D | 0070401 | molecular_function | NADP+ binding |
| D | 0097171 | biological_process | ADP-L-glycero-beta-D-manno-heptose biosynthetic process |
| E | 0005515 | molecular_function | protein binding |
| E | 0005829 | cellular_component | cytosol |
| E | 0005975 | biological_process | carbohydrate metabolic process |
| E | 0008712 | molecular_function | ADP-glyceromanno-heptose 6-epimerase activity |
| E | 0009103 | biological_process | lipopolysaccharide biosynthetic process |
| E | 0009244 | biological_process | lipopolysaccharide core region biosynthetic process |
| E | 0016020 | cellular_component | membrane |
| E | 0016853 | molecular_function | isomerase activity |
| E | 0050661 | molecular_function | NADP binding |
| E | 0070401 | molecular_function | NADP+ binding |
| E | 0097171 | biological_process | ADP-L-glycero-beta-D-manno-heptose biosynthetic process |
| F | 0005515 | molecular_function | protein binding |
| F | 0005829 | cellular_component | cytosol |
| F | 0005975 | biological_process | carbohydrate metabolic process |
| F | 0008712 | molecular_function | ADP-glyceromanno-heptose 6-epimerase activity |
| F | 0009103 | biological_process | lipopolysaccharide biosynthetic process |
| F | 0009244 | biological_process | lipopolysaccharide core region biosynthetic process |
| F | 0016020 | cellular_component | membrane |
| F | 0016853 | molecular_function | isomerase activity |
| F | 0050661 | molecular_function | NADP binding |
| F | 0070401 | molecular_function | NADP+ binding |
| F | 0097171 | biological_process | ADP-L-glycero-beta-D-manno-heptose biosynthetic process |
| G | 0005515 | molecular_function | protein binding |
| G | 0005829 | cellular_component | cytosol |
| G | 0005975 | biological_process | carbohydrate metabolic process |
| G | 0008712 | molecular_function | ADP-glyceromanno-heptose 6-epimerase activity |
| G | 0009103 | biological_process | lipopolysaccharide biosynthetic process |
| G | 0009244 | biological_process | lipopolysaccharide core region biosynthetic process |
| G | 0016020 | cellular_component | membrane |
| G | 0016853 | molecular_function | isomerase activity |
| G | 0050661 | molecular_function | NADP binding |
| G | 0070401 | molecular_function | NADP+ binding |
| G | 0097171 | biological_process | ADP-L-glycero-beta-D-manno-heptose biosynthetic process |
| H | 0005515 | molecular_function | protein binding |
| H | 0005829 | cellular_component | cytosol |
| H | 0005975 | biological_process | carbohydrate metabolic process |
| H | 0008712 | molecular_function | ADP-glyceromanno-heptose 6-epimerase activity |
| H | 0009103 | biological_process | lipopolysaccharide biosynthetic process |
| H | 0009244 | biological_process | lipopolysaccharide core region biosynthetic process |
| H | 0016020 | cellular_component | membrane |
| H | 0016853 | molecular_function | isomerase activity |
| H | 0050661 | molecular_function | NADP binding |
| H | 0070401 | molecular_function | NADP+ binding |
| H | 0097171 | biological_process | ADP-L-glycero-beta-D-manno-heptose biosynthetic process |
| I | 0005515 | molecular_function | protein binding |
| I | 0005829 | cellular_component | cytosol |
| I | 0005975 | biological_process | carbohydrate metabolic process |
| I | 0008712 | molecular_function | ADP-glyceromanno-heptose 6-epimerase activity |
| I | 0009103 | biological_process | lipopolysaccharide biosynthetic process |
| I | 0009244 | biological_process | lipopolysaccharide core region biosynthetic process |
| I | 0016020 | cellular_component | membrane |
| I | 0016853 | molecular_function | isomerase activity |
| I | 0050661 | molecular_function | NADP binding |
| I | 0070401 | molecular_function | NADP+ binding |
| I | 0097171 | biological_process | ADP-L-glycero-beta-D-manno-heptose biosynthetic process |
| J | 0005515 | molecular_function | protein binding |
| J | 0005829 | cellular_component | cytosol |
| J | 0005975 | biological_process | carbohydrate metabolic process |
| J | 0008712 | molecular_function | ADP-glyceromanno-heptose 6-epimerase activity |
| J | 0009103 | biological_process | lipopolysaccharide biosynthetic process |
| J | 0009244 | biological_process | lipopolysaccharide core region biosynthetic process |
| J | 0016020 | cellular_component | membrane |
| J | 0016853 | molecular_function | isomerase activity |
| J | 0050661 | molecular_function | NADP binding |
| J | 0070401 | molecular_function | NADP+ binding |
| J | 0097171 | biological_process | ADP-L-glycero-beta-D-manno-heptose biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE NAP A 2400 |
| Chain | Residue |
| A | GLY6 |
| A | GLY76 |
| A | ALA77 |
| A | SER79 |
| A | ASN92 |
| A | TYR96 |
| A | ALA114 |
| A | SER115 |
| A | SER116 |
| A | TYR140 |
| A | LYS144 |
| A | GLY9 |
| A | TYR167 |
| A | PHE168 |
| A | VAL170 |
| A | HIS177 |
| A | LYS178 |
| A | HOH848 |
| A | HOH1285 |
| A | PHE10 |
| A | ILE11 |
| A | ASP31 |
| A | ASN32 |
| A | LYS38 |
| A | LYS53 |
| A | GLU75 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE ADQ A 2500 |
| Chain | Residue |
| A | THR81 |
| A | ASN169 |
| A | SER180 |
| A | ALA182 |
| A | HIS187 |
| A | ARG209 |
| A | PHE243 |
| site_id | AC3 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE NAP B 2401 |
| Chain | Residue |
| B | GLY6 |
| B | GLY9 |
| B | PHE10 |
| B | ILE11 |
| B | ASP31 |
| B | ASN32 |
| B | LYS38 |
| B | LYS53 |
| B | GLU75 |
| B | GLY76 |
| B | ALA77 |
| B | SER79 |
| B | ASN92 |
| B | TYR96 |
| B | ALA114 |
| B | SER115 |
| B | SER116 |
| B | TYR140 |
| B | LYS144 |
| B | TYR167 |
| B | PHE168 |
| B | VAL170 |
| B | HIS177 |
| B | LYS178 |
| B | HOH648 |
| B | HOH679 |
| B | ADQ2501 |
| site_id | AC4 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE ADQ B 2501 |
| Chain | Residue |
| B | PHE168 |
| B | ASN169 |
| B | SER180 |
| B | ALA182 |
| B | HIS187 |
| B | LEU200 |
| B | PHE201 |
| B | SER204 |
| B | ARG209 |
| B | PHE243 |
| B | TYR272 |
| B | GLN273 |
| B | THR276 |
| B | HOH841 |
| B | HOH981 |
| B | NAP2401 |
| site_id | AC5 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE NAP C 2402 |
| Chain | Residue |
| C | LYS178 |
| C | HOH607 |
| C | GLY6 |
| C | GLY9 |
| C | PHE10 |
| C | ILE11 |
| C | ASP31 |
| C | ASN32 |
| C | LYS38 |
| C | LYS53 |
| C | GLU75 |
| C | GLY76 |
| C | ALA77 |
| C | SER79 |
| C | ASN92 |
| C | TYR96 |
| C | ALA114 |
| C | SER115 |
| C | SER116 |
| C | TYR140 |
| C | LYS144 |
| C | TYR167 |
| C | PHE168 |
| C | VAL170 |
| C | HIS177 |
| site_id | AC6 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE ADQ C 2502 |
| Chain | Residue |
| C | THR81 |
| C | ASN169 |
| C | SER180 |
| C | MET181 |
| C | ALA182 |
| C | VAL184 |
| C | HIS187 |
| C | ARG209 |
| C | PHE243 |
| C | TYR272 |
| site_id | AC7 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE NAP D 2403 |
| Chain | Residue |
| D | GLY6 |
| D | GLY9 |
| D | PHE10 |
| D | ILE11 |
| D | ASP31 |
| D | ASN32 |
| D | LYS38 |
| D | LYS53 |
| D | GLU75 |
| D | GLY76 |
| D | ALA77 |
| D | SER79 |
| D | ASN92 |
| D | TYR96 |
| D | ALA114 |
| D | SER115 |
| D | SER116 |
| D | TYR140 |
| D | LYS144 |
| D | TYR167 |
| D | PHE168 |
| D | VAL170 |
| D | HIS177 |
| D | LYS178 |
| D | HOH601 |
| D | HOH674 |
| D | HOH720 |
| D | ADQ2503 |
| site_id | AC8 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE ADQ D 2503 |
| Chain | Residue |
| D | SER79 |
| D | THR81 |
| D | SER116 |
| D | TYR140 |
| D | ASN169 |
| D | LYS178 |
| D | SER180 |
| D | MET181 |
| D | ALA182 |
| D | VAL184 |
| D | HIS187 |
| D | PHE201 |
| D | SER204 |
| D | ARG209 |
| D | PHE243 |
| D | TYR272 |
| D | HOH820 |
| D | HOH829 |
| D | HOH960 |
| D | HOH1087 |
| D | NAP2403 |
| site_id | AC9 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE NAP E 2404 |
| Chain | Residue |
| E | GLY6 |
| E | GLY9 |
| E | PHE10 |
| E | ILE11 |
| E | ASP31 |
| E | ASN32 |
| E | LYS38 |
| E | LYS53 |
| E | GLU75 |
| E | GLY76 |
| E | ALA77 |
| E | SER79 |
| E | ASN92 |
| E | TYR96 |
| E | ALA114 |
| E | SER115 |
| E | SER116 |
| E | TYR140 |
| E | LYS144 |
| E | TYR167 |
| E | PHE168 |
| E | VAL170 |
| E | HIS177 |
| E | LYS178 |
| E | HOH639 |
| E | HOH671 |
| site_id | BC1 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE ADQ E 2504 |
| Chain | Residue |
| E | ASN169 |
| E | SER180 |
| E | ALA182 |
| E | VAL184 |
| E | HIS187 |
| E | LEU200 |
| E | PHE201 |
| E | SER204 |
| E | ARG209 |
| E | PHE243 |
| E | TYR272 |
| E | GLN273 |
| E | HOH1624 |
| site_id | BC2 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE NAP F 2405 |
| Chain | Residue |
| F | GLY6 |
| F | GLY9 |
| F | PHE10 |
| F | ILE11 |
| F | ASP31 |
| F | ASN32 |
| F | LYS38 |
| F | LYS53 |
| F | GLU75 |
| F | GLY76 |
| F | ALA77 |
| F | SER79 |
| F | ASN92 |
| F | TYR96 |
| F | ALA114 |
| F | SER115 |
| F | SER116 |
| F | TYR140 |
| F | LYS144 |
| F | TYR167 |
| F | PHE168 |
| F | VAL170 |
| F | HIS177 |
| F | LYS178 |
| F | HOH661 |
| F | HOH782 |
| F | HOH809 |
| F | ADQ2505 |
| site_id | BC3 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE ADQ F 2505 |
| Chain | Residue |
| F | ALA117 |
| F | TYR167 |
| F | PHE168 |
| F | ASN169 |
| F | SER180 |
| F | ALA182 |
| F | HIS187 |
| F | LEU200 |
| F | PHE201 |
| F | SER204 |
| F | ARG209 |
| F | PHE243 |
| F | LEU268 |
| F | TYR272 |
| F | GLN273 |
| F | THR276 |
| F | HOH702 |
| F | HOH965 |
| F | HOH1071 |
| F | HOH1262 |
| F | NAP2405 |
| site_id | BC4 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE NAP G 2406 |
| Chain | Residue |
| G | GLY6 |
| G | GLY9 |
| G | PHE10 |
| G | ILE11 |
| G | ASP31 |
| G | ASN32 |
| G | LYS38 |
| G | LYS53 |
| G | GLU75 |
| G | GLY76 |
| G | ALA77 |
| G | SER79 |
| G | ASN92 |
| G | TYR96 |
| G | ALA114 |
| G | SER115 |
| G | SER116 |
| G | TYR140 |
| G | LYS144 |
| G | TYR167 |
| G | PHE168 |
| G | VAL170 |
| G | HIS177 |
| G | LYS178 |
| G | HOH620 |
| G | HOH819 |
| site_id | BC5 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE ADQ G 2506 |
| Chain | Residue |
| G | THR81 |
| G | ASN169 |
| G | SER180 |
| G | MET181 |
| G | ALA182 |
| G | VAL184 |
| G | HIS187 |
| G | PHE201 |
| G | SER204 |
| G | ARG209 |
| G | PHE243 |
| G | TYR272 |
| G | HOH799 |
| G | HOH1338 |
| G | HOH1546 |
| site_id | BC6 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE NAP H 2407 |
| Chain | Residue |
| H | GLY6 |
| H | GLY9 |
| H | PHE10 |
| H | ILE11 |
| H | ASP31 |
| H | ASN32 |
| H | LYS38 |
| H | LYS53 |
| H | GLU75 |
| H | GLY76 |
| H | ALA77 |
| H | SER79 |
| H | TYR88 |
| H | ASN92 |
| H | TYR96 |
| H | ALA114 |
| H | SER115 |
| H | SER116 |
| H | TYR140 |
| H | LYS144 |
| H | TYR167 |
| H | PHE168 |
| H | VAL170 |
| H | HIS177 |
| H | LYS178 |
| H | HOH615 |
| site_id | BC7 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE ADQ H 2507 |
| Chain | Residue |
| H | ASN169 |
| H | SER180 |
| H | VAL184 |
| H | HIS187 |
| H | LEU200 |
| H | PHE201 |
| H | SER204 |
| H | ARG209 |
| H | PHE243 |
| H | TYR272 |
| H | HOH1218 |
| H | HOH1650 |
| site_id | BC8 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE NAP I 2408 |
| Chain | Residue |
| I | GLY6 |
| I | GLY9 |
| I | PHE10 |
| I | ILE11 |
| I | ASP31 |
| I | ASN32 |
| I | LYS38 |
| I | LYS53 |
| I | GLU75 |
| I | GLY76 |
| I | ALA77 |
| I | SER79 |
| I | ASN92 |
| I | TYR96 |
| I | ALA114 |
| I | SER115 |
| I | SER116 |
| I | TYR140 |
| I | LYS144 |
| I | TYR167 |
| I | PHE168 |
| I | VAL170 |
| I | HIS177 |
| I | LYS178 |
| I | HOH624 |
| I | HOH633 |
| I | HOH928 |
| I | HOH947 |
| site_id | BC9 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE ADQ I 2508 |
| Chain | Residue |
| I | THR81 |
| I | ASN169 |
| I | SER180 |
| I | MET181 |
| I | ALA182 |
| I | VAL184 |
| I | HIS187 |
| I | PHE201 |
| I | SER204 |
| I | ARG209 |
| I | PHE243 |
| I | LEU268 |
| I | TYR272 |
| I | HOH742 |
| I | HOH1164 |
| I | HOH1401 |
| I | HOH1561 |
| site_id | CC1 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE NAP J 2409 |
| Chain | Residue |
| J | GLY6 |
| J | GLY9 |
| J | PHE10 |
| J | ILE11 |
| J | ASP31 |
| J | ASN32 |
| J | LYS38 |
| J | LYS53 |
| J | GLU75 |
| J | GLY76 |
| J | ALA77 |
| J | SER79 |
| J | ASN92 |
| J | TYR96 |
| J | ALA114 |
| J | SER115 |
| J | SER116 |
| J | TYR140 |
| J | LYS144 |
| J | TYR167 |
| J | PHE168 |
| J | VAL170 |
| J | HIS177 |
| J | LYS178 |
| J | HOH602 |
| site_id | CC2 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE ADQ J 2509 |
| Chain | Residue |
| J | ASN169 |
| J | SER180 |
| J | ALA182 |
| J | VAL184 |
| J | HIS187 |
| J | LEU200 |
| J | PHE201 |
| J | SER204 |
| J | ARG209 |
| J | PHE243 |
| J | TYR272 |
| J | HOH1602 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 20 |
| Details | ACT_SITE: Proton acceptor => ECO:0000269|PubMed:17316025 |
| Chain | Residue | Details |
| A | TYR140 | |
| E | LYS178 | |
| F | TYR140 | |
| F | LYS178 | |
| G | TYR140 | |
| G | LYS178 | |
| H | TYR140 | |
| H | LYS178 | |
| I | TYR140 | |
| I | LYS178 | |
| J | TYR140 | |
| A | LYS178 | |
| J | LYS178 | |
| B | TYR140 | |
| B | LYS178 | |
| C | TYR140 | |
| C | LYS178 | |
| D | TYR140 | |
| D | LYS178 | |
| E | TYR140 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 150 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:10896473 |
| Chain | Residue | Details |
| A | PHE10 | |
| A | LYS178 | |
| G | LYS178 | |
| G | SER180 | |
| G | HIS187 | |
| G | PHE201 | |
| G | ARG209 | |
| G | TYR272 | |
| H | PHE10 | |
| H | ASP31 | |
| H | LYS38 | |
| H | LYS53 | |
| A | SER180 | |
| H | GLU75 | |
| H | ASN92 | |
| H | LYS144 | |
| H | ASN169 | |
| H | VAL170 | |
| H | LYS178 | |
| H | SER180 | |
| H | HIS187 | |
| H | PHE201 | |
| H | ARG209 | |
| A | HIS187 | |
| H | TYR272 | |
| I | PHE10 | |
| I | ASP31 | |
| I | LYS38 | |
| I | LYS53 | |
| I | GLU75 | |
| I | ASN92 | |
| I | LYS144 | |
| I | ASN169 | |
| I | VAL170 | |
| A | PHE201 | |
| I | LYS178 | |
| I | SER180 | |
| I | HIS187 | |
| I | PHE201 | |
| I | ARG209 | |
| I | TYR272 | |
| J | PHE10 | |
| J | ASP31 | |
| J | LYS38 | |
| J | LYS53 | |
| A | ARG209 | |
| J | GLU75 | |
| J | ASN92 | |
| J | LYS144 | |
| J | ASN169 | |
| J | VAL170 | |
| J | LYS178 | |
| J | SER180 | |
| J | HIS187 | |
| J | PHE201 | |
| J | ARG209 | |
| A | TYR272 | |
| J | TYR272 | |
| B | PHE10 | |
| B | ASP31 | |
| B | LYS38 | |
| B | LYS53 | |
| A | ASP31 | |
| B | GLU75 | |
| B | ASN92 | |
| B | LYS144 | |
| B | ASN169 | |
| B | VAL170 | |
| B | LYS178 | |
| B | SER180 | |
| B | HIS187 | |
| B | PHE201 | |
| B | ARG209 | |
| A | LYS38 | |
| B | TYR272 | |
| C | PHE10 | |
| C | ASP31 | |
| C | LYS38 | |
| C | LYS53 | |
| C | GLU75 | |
| C | ASN92 | |
| C | LYS144 | |
| C | ASN169 | |
| C | VAL170 | |
| A | LYS53 | |
| C | LYS178 | |
| C | SER180 | |
| C | HIS187 | |
| C | PHE201 | |
| C | ARG209 | |
| C | TYR272 | |
| D | PHE10 | |
| D | ASP31 | |
| D | LYS38 | |
| D | LYS53 | |
| A | GLU75 | |
| D | GLU75 | |
| D | ASN92 | |
| D | LYS144 | |
| D | ASN169 | |
| D | VAL170 | |
| D | LYS178 | |
| D | SER180 | |
| D | HIS187 | |
| D | PHE201 | |
| D | ARG209 | |
| A | ASN92 | |
| D | TYR272 | |
| E | PHE10 | |
| E | ASP31 | |
| E | LYS38 | |
| E | LYS53 | |
| E | GLU75 | |
| E | ASN92 | |
| E | LYS144 | |
| E | ASN169 | |
| E | VAL170 | |
| A | LYS144 | |
| E | LYS178 | |
| E | SER180 | |
| E | HIS187 | |
| E | PHE201 | |
| E | ARG209 | |
| E | TYR272 | |
| F | PHE10 | |
| F | ASP31 | |
| F | LYS38 | |
| F | LYS53 | |
| A | ASN169 | |
| F | GLU75 | |
| F | ASN92 | |
| F | LYS144 | |
| F | ASN169 | |
| F | VAL170 | |
| F | LYS178 | |
| F | SER180 | |
| F | HIS187 | |
| F | PHE201 | |
| F | ARG209 | |
| A | VAL170 | |
| F | TYR272 | |
| G | PHE10 | |
| G | ASP31 | |
| G | LYS38 | |
| G | LYS53 | |
| G | GLU75 | |
| G | ASN92 | |
| G | LYS144 | |
| G | ASN169 | |
| G | VAL170 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 10 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18723842 |
| Chain | Residue | Details |
| A | LYS267 | |
| J | LYS267 | |
| B | LYS267 | |
| C | LYS267 | |
| D | LYS267 | |
| E | LYS267 | |
| F | LYS267 | |
| G | LYS267 | |
| H | LYS267 | |
| I | LYS267 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 3 |
| Details | M-CSA 557 |
| Chain | Residue | Details |
| A | SER116 | electrostatic stabiliser, proton acceptor, proton donor, proton relay |
| A | TYR140 | proton acceptor, proton donor |
| A | LYS178 | electrostatic stabiliser, proton acceptor, proton donor |
| site_id | MCSA2 |
| Number of Residues | 3 |
| Details | M-CSA 557 |
| Chain | Residue | Details |
| B | SER116 | electrostatic stabiliser, proton acceptor, proton donor, proton relay |
| B | TYR140 | proton acceptor, proton donor |
| B | LYS178 | electrostatic stabiliser, proton acceptor, proton donor |
| site_id | MCSA3 |
| Number of Residues | 3 |
| Details | M-CSA 557 |
| Chain | Residue | Details |
| C | SER116 | electrostatic stabiliser, proton acceptor, proton donor, proton relay |
| C | TYR140 | proton acceptor, proton donor |
| C | LYS178 | electrostatic stabiliser, proton acceptor, proton donor |
| site_id | MCSA4 |
| Number of Residues | 3 |
| Details | M-CSA 557 |
| Chain | Residue | Details |
| D | SER116 | electrostatic stabiliser, proton acceptor, proton donor, proton relay |
| D | TYR140 | proton acceptor, proton donor |
| D | LYS178 | electrostatic stabiliser, proton acceptor, proton donor |
| site_id | MCSA5 |
| Number of Residues | 3 |
| Details | M-CSA 557 |
| Chain | Residue | Details |
| E | SER116 | electrostatic stabiliser, proton acceptor, proton donor, proton relay |
| E | TYR140 | proton acceptor, proton donor |
| E | LYS178 | electrostatic stabiliser, proton acceptor, proton donor |
| site_id | MCSA6 |
| Number of Residues | 3 |
| Details | M-CSA 557 |
| Chain | Residue | Details |
| F | SER116 | electrostatic stabiliser, proton acceptor, proton donor, proton relay |
| F | TYR140 | proton acceptor, proton donor |
| F | LYS178 | electrostatic stabiliser, proton acceptor, proton donor |
| site_id | MCSA7 |
| Number of Residues | 3 |
| Details | M-CSA 557 |
| Chain | Residue | Details |
| G | SER116 | electrostatic stabiliser, proton acceptor, proton donor, proton relay |
| G | TYR140 | proton acceptor, proton donor |
| G | LYS178 | electrostatic stabiliser, proton acceptor, proton donor |
| site_id | MCSA8 |
| Number of Residues | 3 |
| Details | M-CSA 557 |
| Chain | Residue | Details |
| H | SER116 | electrostatic stabiliser, proton acceptor, proton donor, proton relay |
| H | TYR140 | proton acceptor, proton donor |
| H | LYS178 | electrostatic stabiliser, proton acceptor, proton donor |
| site_id | MCSA9 |
| Number of Residues | 3 |
| Details | M-CSA 557 |
| Chain | Residue | Details |
| I | SER116 | electrostatic stabiliser, proton acceptor, proton donor, proton relay |
| I | TYR140 | proton acceptor, proton donor |
| I | LYS178 | electrostatic stabiliser, proton acceptor, proton donor |
| site_id | MCSA10 |
| Number of Residues | 3 |
| Details | M-CSA 557 |
| Chain | Residue | Details |
| J | SER116 | electrostatic stabiliser, proton acceptor, proton donor, proton relay |
| J | TYR140 | proton acceptor, proton donor |
| J | LYS178 | electrostatic stabiliser, proton acceptor, proton donor |
