2GO4
Crystal structure of Aquifex aeolicus LpxC complexed with TU-514
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 | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 601 |
| Chain | Residue |
| A | HIS79 |
| A | HIS238 |
| A | ASP242 |
| A | TUX901 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 602 |
| Chain | Residue |
| B | HIS79 |
| B | HIS238 |
| B | ASP242 |
| B | TUX902 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE ZN B 603 |
| Chain | Residue |
| B | HIS200 |
| B | HIS58 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 604 |
| Chain | Residue |
| A | HIS58 |
| A | HIS200 |
| A | CL401 |
| A | HOH925 |
| 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 | 3 |
| Details | BINDING SITE FOR RESIDUE CL A 401 |
| Chain | Residue |
| A | HIS58 |
| A | HIS200 |
| A | ZN604 |
| site_id | AC7 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE TUX A 901 |
| Chain | Residue |
| A | HIS19 |
| A | HIS58 |
| A | GLU78 |
| A | HIS79 |
| A | THR191 |
| A | PHE192 |
| A | GLU197 |
| A | ILE198 |
| A | ILE201 |
| A | GLY207 |
| A | LEU212 |
| A | VAL217 |
| A | HIS238 |
| A | LYS239 |
| A | ASP242 |
| A | HIS265 |
| A | ZN601 |
| A | HOH915 |
| A | HOH924 |
| B | TUX902 |
| site_id | AC8 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE TUX B 902 |
| Chain | Residue |
| A | TUX901 |
| B | ILE18 |
| B | HIS19 |
| B | HIS58 |
| B | GLU78 |
| B | HIS79 |
| B | THR191 |
| B | GLU197 |
| B | ILE201 |
| B | GLY210 |
| B | SER211 |
| B | LEU212 |
| B | HIS238 |
| B | LYS239 |
| B | ASP242 |
| B | HIS265 |
| B | ZN602 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_00388, ECO:0000305|PubMed:15705580 |
| Chain | Residue | Details |
| A | HIS265 | |
| B | HIS265 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00388, ECO:0000269|PubMed:12819349, ECO:0000269|PubMed:15705580, ECO:0007744|PDB:1P42, ECO:0007744|PDB:1YH8, ECO:0007744|PDB:1YHC |
| Chain | Residue | Details |
| A | HIS79 | |
| A | HIS238 | |
| A | ASP242 | |
| B | HIS79 | |
| B | HIS238 | |
| B | ASP242 |
