2IER
Crystal Structure of Aquifex aeolicus LpxC Complexed with Uridine 5'-Diphosphate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0006796 | biological_process | phosphate-containing compound metabolic process |
| A | 0009245 | biological_process | lipid A biosynthetic process |
| A | 0016020 | cellular_component | membrane |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0019637 | biological_process | organophosphate metabolic process |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0103117 | molecular_function | UDP-3-O-acyl-N-acetylglucosamine deacetylase activity |
| A | 1901135 | biological_process | carbohydrate derivative metabolic process |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006629 | biological_process | lipid metabolic process |
| B | 0006796 | biological_process | phosphate-containing compound metabolic process |
| B | 0009245 | biological_process | lipid A biosynthetic process |
| B | 0016020 | cellular_component | membrane |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0019637 | biological_process | organophosphate metabolic process |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0103117 | molecular_function | UDP-3-O-acyl-N-acetylglucosamine deacetylase activity |
| B | 1901135 | biological_process | carbohydrate derivative metabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 601 |
| Chain | Residue |
| A | HIS79 |
| A | HIS238 |
| A | ASP242 |
| A | ZN606 |
| A | HOH802 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN B 602 |
| Chain | Residue |
| B | HOH808 |
| B | HIS79 |
| B | HIS238 |
| B | ASP242 |
| B | ZN607 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE ZN A 603 |
| Chain | Residue |
| A | HIS58 |
| A | HIS200 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE ZN B 604 |
| Chain | Residue |
| B | HIS58 |
| B | HIS200 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 605 |
| Chain | Residue |
| A | GLY2 |
| A | GLU126 |
| B | ILE27 |
| B | HIS29 |
| B | GLU95 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 606 |
| Chain | Residue |
| A | GLU78 |
| A | HIS265 |
| A | ZN601 |
| A | HOH802 |
| A | HOH830 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN B 607 |
| Chain | Residue |
| B | HIS58 |
| B | SER59 |
| B | GLU78 |
| B | HIS265 |
| B | ZN602 |
| B | HOH808 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ZN A 608 |
| Chain | Residue |
| A | HIS58 |
| A | PLM701 |
| A | UDP801 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ZN B 609 |
| Chain | Residue |
| B | HIS58 |
| B | PLM702 |
| B | UDP802 |
| site_id | BC1 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE UDP A 801 |
| Chain | Residue |
| A | HIS58 |
| A | TYR157 |
| A | GLY159 |
| A | GLU160 |
| A | PHE161 |
| A | GLU197 |
| A | LYS239 |
| A | ARG262 |
| A | GLY264 |
| A | HIS265 |
| A | ZN608 |
| A | PLM701 |
| A | HOH808 |
| A | HOH817 |
| A | HOH830 |
| A | HOH837 |
| A | HOH840 |
| site_id | BC2 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE UDP B 802 |
| Chain | Residue |
| B | HIS58 |
| B | TYR157 |
| B | GLY159 |
| B | GLU160 |
| B | PHE161 |
| B | PHE194 |
| B | GLU197 |
| B | LYS239 |
| B | ARG262 |
| B | GLY264 |
| B | HIS265 |
| B | ZN609 |
| B | HOH810 |
| site_id | BC3 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE PLM A 701 |
| Chain | Residue |
| A | ILE18 |
| A | HIS19 |
| A | PHE192 |
| A | GLU197 |
| A | ILE198 |
| A | GLY210 |
| A | ZN608 |
| A | UDP801 |
| A | HOH843 |
| B | SER211 |
| B | LEU212 |
| B | PLM702 |
| site_id | BC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PLM B 702 |
| Chain | Residue |
| A | TYR224 |
| A | PLM701 |
| B | ILE18 |
| B | HIS19 |
| B | ILE198 |
| B | GLY210 |
| B | SER211 |
| B | TYR224 |
| B | ZN609 |
| site_id | BC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 501 |
| Chain | Residue |
| A | HIS85 |
| A | GLU88 |
| A | LEU153 |
| A | VAL254 |
| A | LYS255 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"HAMAP-Rule","id":"MF_00388","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15705580","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00388","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12819349","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15705580","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1P42","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1YH8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1YHC","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
