4ZAH
Crystal structure of sugar aminotransferase WecE with External Aldimine VII from Escherichia coli K-12
Replaces: 4WFPFunctional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000271 | biological_process | polysaccharide biosynthetic process |
| A | 0009246 | biological_process | enterobacterial common antigen biosynthetic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0019180 | molecular_function | dTDP-4-amino-4,6-dideoxygalactose transaminase activity |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0042802 | molecular_function | identical protein binding |
| B | 0000271 | biological_process | polysaccharide biosynthetic process |
| B | 0009246 | biological_process | enterobacterial common antigen biosynthetic process |
| B | 0016740 | molecular_function | transferase activity |
| B | 0019180 | molecular_function | dTDP-4-amino-4,6-dideoxygalactose transaminase activity |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0042802 | molecular_function | identical protein binding |
| C | 0000271 | biological_process | polysaccharide biosynthetic process |
| C | 0009246 | biological_process | enterobacterial common antigen biosynthetic process |
| C | 0016740 | molecular_function | transferase activity |
| C | 0019180 | molecular_function | dTDP-4-amino-4,6-dideoxygalactose transaminase activity |
| C | 0030170 | molecular_function | pyridoxal phosphate binding |
| C | 0042802 | molecular_function | identical protein binding |
| D | 0000271 | biological_process | polysaccharide biosynthetic process |
| D | 0009246 | biological_process | enterobacterial common antigen biosynthetic process |
| D | 0016740 | molecular_function | transferase activity |
| D | 0019180 | molecular_function | dTDP-4-amino-4,6-dideoxygalactose transaminase activity |
| D | 0030170 | molecular_function | pyridoxal phosphate binding |
| D | 0042802 | molecular_function | identical protein binding |
| E | 0000271 | biological_process | polysaccharide biosynthetic process |
| E | 0009246 | biological_process | enterobacterial common antigen biosynthetic process |
| E | 0016740 | molecular_function | transferase activity |
| E | 0019180 | molecular_function | dTDP-4-amino-4,6-dideoxygalactose transaminase activity |
| E | 0030170 | molecular_function | pyridoxal phosphate binding |
| E | 0042802 | molecular_function | identical protein binding |
| F | 0000271 | biological_process | polysaccharide biosynthetic process |
| F | 0009246 | biological_process | enterobacterial common antigen biosynthetic process |
| F | 0016740 | molecular_function | transferase activity |
| F | 0019180 | molecular_function | dTDP-4-amino-4,6-dideoxygalactose transaminase activity |
| F | 0030170 | molecular_function | pyridoxal phosphate binding |
| F | 0042802 | molecular_function | identical protein binding |
| G | 0000271 | biological_process | polysaccharide biosynthetic process |
| G | 0009246 | biological_process | enterobacterial common antigen biosynthetic process |
| G | 0016740 | molecular_function | transferase activity |
| G | 0019180 | molecular_function | dTDP-4-amino-4,6-dideoxygalactose transaminase activity |
| G | 0030170 | molecular_function | pyridoxal phosphate binding |
| G | 0042802 | molecular_function | identical protein binding |
| H | 0000271 | biological_process | polysaccharide biosynthetic process |
| H | 0009246 | biological_process | enterobacterial common antigen biosynthetic process |
| H | 0016740 | molecular_function | transferase activity |
| H | 0019180 | molecular_function | dTDP-4-amino-4,6-dideoxygalactose transaminase activity |
| H | 0030170 | molecular_function | pyridoxal phosphate binding |
| H | 0042802 | molecular_function | identical protein binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 31 |
| Details | binding site for residue T5K A 500 |
| Chain | Residue |
| A | PHE4 |
| A | SER176 |
| A | HIS178 |
| A | THR180 |
| A | LYS181 |
| A | GLY189 |
| A | VAL318 |
| A | PHE319 |
| A | HIS320 |
| A | TYR321 |
| A | ARG352 |
| A | SER54 |
| A | HOH637 |
| A | HOH651 |
| A | HOH670 |
| A | HOH675 |
| A | HOH677 |
| A | HOH683 |
| A | HOH720 |
| A | HOH727 |
| B | ARG213 |
| B | TYR224 |
| A | CYS55 |
| B | HOH623 |
| B | HOH634 |
| A | THR56 |
| A | PHE81 |
| A | VAL126 |
| A | ASP152 |
| A | ALA154 |
| A | GLN155 |
| site_id | AC2 |
| Number of Residues | 25 |
| Details | binding site for residue T5K B 500 |
| Chain | Residue |
| A | TYR224 |
| A | HOH641 |
| B | PHE4 |
| B | SER54 |
| B | CYS55 |
| B | THR56 |
| B | PHE81 |
| B | ASP152 |
| B | ALA154 |
| B | GLN155 |
| B | SER176 |
| B | HIS178 |
| B | LYS181 |
| B | GLY189 |
| B | VAL318 |
| B | PHE319 |
| B | HIS320 |
| B | TYR321 |
| B | ILE322 |
| B | ARG352 |
| B | HOH601 |
| B | HOH627 |
| B | HOH639 |
| B | HOH664 |
| B | HOH682 |
| site_id | AC3 |
| Number of Residues | 26 |
| Details | binding site for residue T5K C 500 |
| Chain | Residue |
| C | SER54 |
| C | CYS55 |
| C | THR56 |
| C | PHE81 |
| C | VAL126 |
| C | ASP152 |
| C | ALA154 |
| C | GLN155 |
| C | SER176 |
| C | HIS178 |
| C | LYS181 |
| C | GLY189 |
| C | VAL318 |
| C | PHE319 |
| C | HIS320 |
| C | TYR321 |
| C | ILE322 |
| C | ARG352 |
| C | HOH603 |
| C | HOH613 |
| C | HOH628 |
| C | HOH656 |
| C | HOH682 |
| D | ARG213 |
| D | LYS223 |
| D | TYR224 |
| site_id | AC4 |
| Number of Residues | 21 |
| Details | binding site for residue T5K D 500 |
| Chain | Residue |
| D | ARG352 |
| D | HOH623 |
| D | HOH632 |
| D | HOH660 |
| C | TYR224 |
| D | PHE4 |
| D | SER54 |
| D | CYS55 |
| D | THR56 |
| D | PHE81 |
| D | VAL126 |
| D | ASP152 |
| D | ALA154 |
| D | GLN155 |
| D | SER176 |
| D | LYS181 |
| D | GLY189 |
| D | VAL318 |
| D | PHE319 |
| D | HIS320 |
| D | TYR321 |
| site_id | AC5 |
| Number of Residues | 23 |
| Details | binding site for residue T5K E 500 |
| Chain | Residue |
| E | SER54 |
| E | CYS55 |
| E | THR56 |
| E | THR80 |
| E | PHE81 |
| E | VAL126 |
| E | ASP152 |
| E | ALA154 |
| E | GLN155 |
| E | SER176 |
| E | HIS178 |
| E | LYS181 |
| E | GLY189 |
| E | VAL318 |
| E | PHE319 |
| E | HIS320 |
| E | TYR321 |
| E | ARG352 |
| E | HOH605 |
| E | HOH650 |
| E | HOH671 |
| F | ARG213 |
| F | TYR224 |
| site_id | AC6 |
| Number of Residues | 23 |
| Details | binding site for residue T5K F 500 |
| Chain | Residue |
| E | TYR224 |
| F | PHE4 |
| F | SER54 |
| F | CYS55 |
| F | THR56 |
| F | THR80 |
| F | PHE81 |
| F | ASP152 |
| F | ALA154 |
| F | GLN155 |
| F | SER176 |
| F | HIS178 |
| F | THR180 |
| F | LYS181 |
| F | GLY189 |
| F | VAL318 |
| F | PHE319 |
| F | HIS320 |
| F | TYR321 |
| F | ARG352 |
| F | HOH601 |
| F | HOH602 |
| F | HOH606 |
| site_id | AC7 |
| Number of Residues | 23 |
| Details | binding site for residue T5K G 500 |
| Chain | Residue |
| G | PHE4 |
| G | SER54 |
| G | CYS55 |
| G | THR56 |
| G | THR80 |
| G | PHE81 |
| G | ASP152 |
| G | ALA154 |
| G | GLN155 |
| G | SER176 |
| G | HIS178 |
| G | THR180 |
| G | LYS181 |
| G | GLY189 |
| G | VAL318 |
| G | PHE319 |
| G | HIS320 |
| G | TYR321 |
| G | ILE322 |
| G | ARG352 |
| G | HOH607 |
| H | ARG213 |
| H | TYR224 |
| site_id | AC8 |
| Number of Residues | 22 |
| Details | binding site for residue T5K H 500 |
| Chain | Residue |
| G | TYR224 |
| H | SER54 |
| H | CYS55 |
| H | THR56 |
| H | PHE81 |
| H | VAL126 |
| H | ASP152 |
| H | ALA154 |
| H | GLN155 |
| H | SER176 |
| H | HIS178 |
| H | THR180 |
| H | LYS181 |
| H | GLY189 |
| H | VAL318 |
| H | PHE319 |
| H | HIS320 |
| H | TYR321 |
| H | ILE322 |
| H | ARG352 |
| H | HOH612 |
| H | HOH613 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"UniProtKB","id":"Q8ZNF3","evidenceCode":"ECO:0000250"},{"source":"HAMAP-Rule","id":"MF_02026","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |






