8ALK
Structure of the Legionella phosphocholine hydrolase Lem3 in complex with its substrate Rab1
Functional Information from GO Data
Functional Information from PROSITE/UniProt
site_id | PS00675 |
Number of Residues | 14 |
Details | SIGMA54_INTERACT_1 Sigma-54 interaction domain ATP-binding region A signature. LLLiGDSGVGKscL |
Chain | Residue | Details |
B | LEU11-LEU24 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000269|PubMed:20064470, ECO:0000269|PubMed:20651120, ECO:0000269|PubMed:23236136, ECO:0000269|PubMed:27552051, ECO:0007744|PDB:3JZA, ECO:0007744|PDB:3NKV, ECO:0007744|PDB:4HLQ, ECO:0007744|PDB:4I1O, ECO:0007744|PDB:5SZH, ECO:0007744|PDB:5SZK |
Chain | Residue | Details |
B | GLY15 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000269|PubMed:20651120, ECO:0000269|PubMed:23236136, ECO:0000269|PubMed:27552051, ECO:0007744|PDB:3NKV, ECO:0007744|PDB:4HLQ, ECO:0007744|PDB:5SZH, ECO:0007744|PDB:5SZK |
Chain | Residue | Details |
B | TYR33 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000269|PubMed:20651120, ECO:0000269|PubMed:27552051, ECO:0007744|PDB:3NKV, ECO:0007744|PDB:5SZH, ECO:0007744|PDB:5SZK |
Chain | Residue | Details |
B | ASP63 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:20651120, ECO:0000269|PubMed:23236136, ECO:0000269|PubMed:27552051, ECO:0007744|PDB:3NKV, ECO:0007744|PDB:4HLQ, ECO:0007744|PDB:4I1O, ECO:0007744|PDB:5SZH, ECO:0007744|PDB:5SZK |
Chain | Residue | Details |
B | ASN121 | |
B | SER151 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | MOD_RES: (Microbial infection) O-(2-cholinephosphoryl)serine => ECO:0000269|PubMed:21822290, ECO:0000269|PubMed:22158903, ECO:0000269|PubMed:22307087 |
Chain | Residue | Details |
B | THR76 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | MOD_RES: (Microbial infection) O-AMP-tyrosine => ECO:0000269|PubMed:20651120 |
Chain | Residue | Details |
B | TYR77 |