2IES
Crystal Structure of Aquifex aeolicus LpxC Complexed with Pyrophosphate
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 602 |
Chain | Residue |
A | CL608 |
B | HIS58 |
B | POP700 |
B | PLM802 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 603 |
Chain | Residue |
A | HIS79 |
A | HIS238 |
A | ASP242 |
A | PLM801 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE POP A 701 |
Chain | Residue |
A | HIS58 |
A | LYS239 |
A | HIS265 |
A | ZN604 |
A | ASN57 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 604 |
Chain | Residue |
A | HIS58 |
A | CL607 |
A | POP701 |
A | PLM801 |
site_id | AC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE ZN A 606 |
Chain | Residue |
A | VAL254 |
A | LYS255 |
A | HOH814 |
site_id | AC6 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE PLM A 801 |
Chain | Residue |
A | HIS58 |
A | GLU78 |
A | HIS79 |
A | THR191 |
A | ILE198 |
A | HIS238 |
A | ASP242 |
A | HIS265 |
A | ZN603 |
A | ZN604 |
A | CL607 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 605 |
Chain | Residue |
B | HIS79 |
B | HIS238 |
B | ASP242 |
B | PLM802 |
site_id | AC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CL A 607 |
Chain | Residue |
A | PHE192 |
A | GLU197 |
A | ZN604 |
A | PLM801 |
site_id | AC9 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE POP B 700 |
Chain | Residue |
A | ZN602 |
B | ASN57 |
B | HIS58 |
B | LYS239 |
B | HIS265 |
B | PLM802 |
B | HOH806 |
B | HOH807 |
site_id | BC1 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE PLM B 802 |
Chain | Residue |
A | ZN602 |
A | ZN605 |
A | CL608 |
B | HIS58 |
B | GLU78 |
B | HIS79 |
B | THR191 |
B | ILE198 |
B | ILE201 |
B | GLY210 |
B | SER211 |
B | LEU212 |
B | HIS238 |
B | ASP242 |
B | HIS265 |
B | POP700 |
site_id | BC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL A 608 |
Chain | Residue |
A | ZN602 |
B | GLU197 |
B | PLM802 |
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 |