1YH8
Crystal structure of Aquifex aeolicus LpxC deacetylase complexed with palmitate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0006796 | biological_process | phosphate-containing compound metabolic process |
| A | 0008759 | molecular_function | UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase activity |
| A | 0009245 | biological_process | lipid A biosynthetic process |
| 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 | 0006796 | biological_process | phosphate-containing compound metabolic process |
| B | 0008759 | molecular_function | UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase activity |
| B | 0009245 | biological_process | lipid A biosynthetic process |
| 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 501 |
| Chain | Residue |
| A | HIS79 |
| A | HIS238 |
| A | ASP242 |
| A | PAM801 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE ZN A 503 |
| Chain | Residue |
| A | HIS58 |
| A | HIS200 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 504 |
| Chain | Residue |
| B | GLY2 |
| B | GLU126 |
| A | ILE27 |
| A | HIS29 |
| A | GLU95 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 505 |
| Chain | Residue |
| B | HIS79 |
| B | HIS238 |
| B | ASP242 |
| B | PAM802 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 507 |
| Chain | Residue |
| B | HIS58 |
| B | HIS200 |
| B | CL603 |
| B | HOH863 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL A 601 |
| Chain | Residue |
| A | HIS79 |
| A | ILE103 |
| A | SER107 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL B 602 |
| Chain | Residue |
| B | GLY15 |
| B | VAL16 |
| B | ILE103 |
| B | LEU104 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL B 603 |
| Chain | Residue |
| B | HIS58 |
| B | HIS200 |
| B | ZN507 |
| site_id | AC9 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PAM A 801 |
| Chain | Residue |
| A | ILE18 |
| A | HIS58 |
| A | GLU78 |
| A | HIS79 |
| A | THR191 |
| A | GLY210 |
| A | HIS238 |
| A | ASP242 |
| A | HIS265 |
| A | ZN501 |
| site_id | BC1 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE PAM B 802 |
| Chain | Residue |
| A | LEU212 |
| B | ILE18 |
| B | HIS58 |
| B | GLU78 |
| B | HIS79 |
| B | THR191 |
| B | SER211 |
| B | HIS238 |
| B | ASP242 |
| B | HIS265 |
| B | ZN505 |
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 |
