2GO3
Crystal structure of Aquifex aeolicus LpxC complexed with imidazole.
Functional Information from GO Data
Chain | GOid | namespace | contents |
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 | 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 | 6 |
Details | BINDING SITE FOR RESIDUE ZN B 601 |
Chain | Residue |
B | HIS79 |
B | HIS238 |
B | ASP242 |
B | IMD804 |
B | HOH1117 |
B | HOH1118 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE ZN A 602 |
Chain | Residue |
A | IMD803 |
A | HOH1094 |
A | HOH1095 |
A | HIS79 |
A | HIS238 |
A | ASP242 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN B 603 |
Chain | Residue |
A | HIS29 |
A | GLU95 |
B | GLY2 |
B | GLU126 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 604 |
Chain | Residue |
A | HIS58 |
A | HIS200 |
A | CL607 |
A | IMD801 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN B 605 |
Chain | Residue |
B | HIS58 |
B | HIS200 |
B | CL606 |
B | IMD802 |
site_id | AC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL B 606 |
Chain | Residue |
B | PHE167 |
B | ZN605 |
B | IMD802 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CL A 607 |
Chain | Residue |
A | PHE167 |
A | ZN604 |
A | IMD801 |
A | HOH1049 |
site_id | AC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PLM A 701 |
Chain | Residue |
A | HIS58 |
A | ILE198 |
A | TYR224 |
B | ILE198 |
B | MYR702 |
site_id | AC9 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE MYR B 702 |
Chain | Residue |
A | PLM701 |
B | ILE18 |
B | HIS58 |
B | PHE192 |
B | GLY210 |
B | HOH905 |
B | HOH972 |
B | HOH1049 |
site_id | BC1 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE MYR A 703 |
Chain | Residue |
A | LYS202 |
A | GLY210 |
A | SER211 |
A | LEU212 |
A | LYS213 |
A | HOH962 |
A | HOH1044 |
A | HOH1096 |
B | LYS202 |
B | GLY210 |
B | SER211 |
B | LEU212 |
B | LYS213 |
B | HOH919 |
site_id | BC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE IMD A 801 |
Chain | Residue |
A | HIS58 |
A | PHE167 |
A | HIS200 |
A | ZN604 |
A | CL607 |
site_id | BC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE IMD B 802 |
Chain | Residue |
B | HIS58 |
B | PHE167 |
B | HIS200 |
B | ZN605 |
B | CL606 |
site_id | BC4 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE IMD A 803 |
Chain | Residue |
A | HIS58 |
A | GLU78 |
A | HIS79 |
A | THR191 |
A | HIS238 |
A | ASP242 |
A | HIS265 |
A | ZN602 |
A | HOH1094 |
A | HOH1095 |
site_id | BC5 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE IMD B 804 |
Chain | Residue |
B | HIS58 |
B | GLU78 |
B | HIS79 |
B | THR191 |
B | HIS238 |
B | ASP242 |
B | HIS265 |
B | ZN601 |
B | HOH1117 |
B | HOH1118 |
site_id | BC6 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GOL B 901 |
Chain | Residue |
B | HIS85 |
B | LEU86 |
B | GLU88 |
B | TYR129 |
B | LEU153 |
B | VAL254 |
B | LYS255 |
B | HOH941 |
B | HOH1119 |
site_id | BC7 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL A 902 |
Chain | Residue |
A | GLU88 |
A | LEU153 |
A | VAL254 |
A | LYS255 |
A | HOH992 |
A | HIS85 |
A | LEU86 |
site_id | BC8 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GOL B 903 |
Chain | Residue |
B | VAL53 |
B | VAL54 |
B | HIS55 |
B | GLU158 |
B | ARG170 |
B | LYS172 |
B | LYS273 |
B | HOH976 |
B | HOH1097 |
site_id | BC9 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL B 904 |
Chain | Residue |
A | LYS10 |
A | HIS29 |
B | TYR129 |
B | ASP151 |
B | HOH984 |
B | HOH1084 |
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 |