5KLQ
Crystal structure of HopZ1a in complex with IP6 and CoA
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000822 | molecular_function | inositol hexakisphosphate binding |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005576 | cellular_component | extracellular region |
| A | 0016407 | molecular_function | acetyltransferase activity |
| A | 0016413 | molecular_function | O-acetyltransferase activity |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016746 | molecular_function | acyltransferase activity |
| A | 0020002 | cellular_component | host cell plasma membrane |
| A | 0035821 | biological_process | modulation of process of another organism |
| A | 0042025 | cellular_component | host cell nucleus |
| A | 0044163 | cellular_component | host cytoskeleton |
| A | 0090729 | molecular_function | toxin activity |
| B | 0000822 | molecular_function | inositol hexakisphosphate binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005576 | cellular_component | extracellular region |
| B | 0016407 | molecular_function | acetyltransferase activity |
| B | 0016413 | molecular_function | O-acetyltransferase activity |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016746 | molecular_function | acyltransferase activity |
| B | 0020002 | cellular_component | host cell plasma membrane |
| B | 0035821 | biological_process | modulation of process of another organism |
| B | 0042025 | cellular_component | host cell nucleus |
| B | 0044163 | cellular_component | host cytoskeleton |
| B | 0090729 | molecular_function | toxin activity |
| C | 0000822 | molecular_function | inositol hexakisphosphate binding |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0005515 | molecular_function | protein binding |
| C | 0005576 | cellular_component | extracellular region |
| C | 0016407 | molecular_function | acetyltransferase activity |
| C | 0016413 | molecular_function | O-acetyltransferase activity |
| C | 0016740 | molecular_function | transferase activity |
| C | 0016746 | molecular_function | acyltransferase activity |
| C | 0020002 | cellular_component | host cell plasma membrane |
| C | 0035821 | biological_process | modulation of process of another organism |
| C | 0042025 | cellular_component | host cell nucleus |
| C | 0044163 | cellular_component | host cytoskeleton |
| C | 0090729 | molecular_function | toxin activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 14 |
| Details | binding site for residue IHP C 401 |
| Chain | Residue |
| C | LYS53 |
| C | HIS317 |
| C | ARG326 |
| C | PHE355 |
| C | GLN358 |
| C | ARG362 |
| C | ARG106 |
| C | ASN222 |
| C | ILE225 |
| C | LYS226 |
| C | LYS229 |
| C | LYS289 |
| C | HIS290 |
| C | SER314 |
| site_id | AC2 |
| Number of Residues | 15 |
| Details | binding site for residue COA C 402 |
| Chain | Residue |
| C | ALA172 |
| C | VAL173 |
| C | GLY176 |
| C | ALA177 |
| C | GLN181 |
| C | LYS211 |
| C | THR212 |
| C | SER293 |
| C | LEU294 |
| C | THR295 |
| C | ARG331 |
| C | ARG334 |
| C | ASN345 |
| C | GLN347 |
| C | PHE348 |
| site_id | AC3 |
| Number of Residues | 16 |
| Details | binding site for residue IHP A 401 |
| Chain | Residue |
| A | ARG49 |
| A | LYS53 |
| A | ARG106 |
| A | ASN222 |
| A | ILE225 |
| A | LYS226 |
| A | LYS229 |
| A | LYS289 |
| A | HIS290 |
| A | ASN313 |
| A | SER314 |
| A | HIS317 |
| A | ARG326 |
| A | PHE355 |
| A | GLN358 |
| A | ARG362 |
| site_id | AC4 |
| Number of Residues | 13 |
| Details | binding site for residue COA A 402 |
| Chain | Residue |
| A | HIS150 |
| A | ALA172 |
| A | LYS211 |
| A | THR212 |
| A | SER213 |
| A | SER293 |
| A | LEU294 |
| A | THR295 |
| A | ARG331 |
| A | ARG334 |
| A | SER344 |
| A | GLN347 |
| A | PHE348 |
| site_id | AC5 |
| Number of Residues | 13 |
| Details | binding site for residue IHP B 401 |
| Chain | Residue |
| B | LYS53 |
| B | ARG106 |
| B | ASN222 |
| B | LYS226 |
| B | LYS229 |
| B | LYS289 |
| B | ASN313 |
| B | SER314 |
| B | HIS317 |
| B | ARG326 |
| B | PHE355 |
| B | GLN358 |
| B | ARG362 |
| site_id | AC6 |
| Number of Residues | 11 |
| Details | binding site for residue COA B 402 |
| Chain | Residue |
| B | LYS211 |
| B | THR212 |
| B | ALA292 |
| B | SER293 |
| B | LEU294 |
| B | THR295 |
| B | ARG334 |
| B | ARG335 |
| B | SER344 |
| B | GLN347 |
| B | PHE348 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue CIT B 403 |
| Chain | Residue |
| A | ARG62 |
| A | HIS63 |
| B | HIS150 |
| B | ARG184 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | Active site: {"evidences":[{"source":"PubMed","id":"27525589","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | Active site: {"evidences":[{"source":"PubMed","id":"27525589","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22319451","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PDB","id":"5KLP","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 39 |
| Details | Binding site: {"evidences":[{"source":"PDB","id":"5KLP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5KLQ","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 39 |
| Details | Binding site: {"evidences":[{"source":"PDB","id":"5KLQ","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 3 |
| Details | Modified residue: {"description":"N6-acetyllysine; by autocatalysis","evidences":[{"source":"PubMed","id":"22319451","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26217317","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
