2O3Z
X-ray crystal structure of LpxC complexed with 3-heptyloxybenzoate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0006796 | biological_process | phosphate-containing compound metabolic process |
| A | 0008759 | molecular_function | obsolete 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 | obsolete 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 | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 A 401 |
| Chain | Residue |
| A | THR56 |
| A | HIS58 |
| A | LYS239 |
| A | GLY264 |
| A | HIS265 |
| A | HOH622 |
| A | HOH668 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 B 401 |
| Chain | Residue |
| B | LYS239 |
| B | GLY264 |
| B | HIS265 |
| B | AI7301 |
| B | THR56 |
| B | HIS58 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ZN A 501 |
| Chain | Residue |
| A | HIS79 |
| A | HIS238 |
| A | ASP242 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 502 |
| Chain | Residue |
| A | HIS58 |
| A | HIS200 |
| A | CL601 |
| A | HOH602 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ZN B 503 |
| Chain | Residue |
| B | HIS79 |
| B | HIS238 |
| B | ASP242 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 504 |
| Chain | Residue |
| B | HIS58 |
| B | HIS200 |
| B | HOH507 |
| B | HOH508 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 506 |
| Chain | Residue |
| A | GLY2 |
| A | GLU126 |
| B | HIS29 |
| B | GLU95 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL A 601 |
| Chain | Residue |
| A | PHE167 |
| A | HIS200 |
| A | ZN502 |
| site_id | AC9 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE AI7 A 301 |
| Chain | Residue |
| A | ILE18 |
| A | ILE198 |
| A | LYS202 |
| A | GLY210 |
| A | SER211 |
| A | HOH667 |
| A | HOH699 |
| B | SER211 |
| B | LEU212 |
| B | AI7301 |
| site_id | BC1 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE AI7 B 301 |
| Chain | Residue |
| A | LEU212 |
| A | AI7301 |
| B | ILE18 |
| B | ILE198 |
| B | ILE201 |
| B | LYS202 |
| B | GLY207 |
| B | GLY210 |
| B | SER211 |
| B | VAL217 |
| B | SO4401 |
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 |
