2CHF
STRUCTURE OF THE MG2+-BOUND FORM OF CHEY AND THE MECHANISM OF PHOSPHORYL TRANSFER IN BACTERIAL CHEMOTAXIS
Functional Information from GO Data
Functional Information from PDB Data
site_id | CAT |
Number of Residues | 5 |
Details | CATALYTIC site |
Chain | Residue |
A | ASP12 |
A | ASP13 |
A | ASP57 |
A | ASN59 |
A | LYS109 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:A0A0H3AMJ9 |
Chain | Residue | Details |
A | ASP13 |
site_id | SWS_FT_FI2 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000269|PubMed:16674976, ECO:0000269|PubMed:18083806, ECO:0000269|PubMed:8257674, ECO:0007744|PDB:2CHE, ECO:0007744|PDB:2FKA, ECO:0007744|PDB:2FLW, ECO:0007744|PDB:2FMH, ECO:0007744|PDB:2FMK, ECO:0007744|PDB:2PL9, ECO:0007744|PDB:2PMC |
Chain | Residue | Details |
A | PHE14 | |
A | TRP58 | |
A | MET60 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | MOD_RES: 4-aspartylphosphate => ECO:0000255|PROSITE-ProRule:PRU00169, ECO:0000269|PubMed:1902474, ECO:0000269|PubMed:3280143 |
Chain | Residue | Details |
A | TRP58 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | MOD_RES: N6-acetyllysine => ECO:0000250 |
Chain | Residue | Details |
A | GLU93 | |
A | PRO110 |