6EQL
Crystal Structure of Human Glycogenin-1 (GYG1) Tyr195pIPhe mutant complexed with manganese and UDP
Functional Information from GO Data
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 14 |
Details | binding site for residue UDP A 301 |
Chain | Residue |
A | LEU9 |
A | HIS212 |
A | LEU214 |
A | GLY215 |
A | LYS218 |
A | MN302 |
A | THR10 |
A | THR11 |
A | ASN12 |
A | TYR15 |
A | ARG30 |
A | ASP102 |
A | ALA103 |
A | ASP104 |
site_id | AC2 |
Number of Residues | 4 |
Details | binding site for residue MN A 302 |
Chain | Residue |
A | ASP102 |
A | ASP104 |
A | HIS212 |
A | UDP301 |
site_id | AC3 |
Number of Residues | 16 |
Details | binding site for residue UDP B 301 |
Chain | Residue |
B | LEU9 |
B | THR10 |
B | THR11 |
B | ASN12 |
B | TYR15 |
B | VAL82 |
B | ASP102 |
B | ALA103 |
B | ASP104 |
B | HIS212 |
B | LEU214 |
B | GLY215 |
B | LYS218 |
B | MN302 |
B | 2PE303 |
B | EDO304 |
site_id | AC4 |
Number of Residues | 4 |
Details | binding site for residue MN B 302 |
Chain | Residue |
B | ASP102 |
B | ASP104 |
B | HIS212 |
B | UDP301 |
site_id | AC5 |
Number of Residues | 10 |
Details | binding site for residue 2PE B 303 |
Chain | Residue |
B | ASP125 |
B | ASN133 |
B | SER134 |
B | GLY162 |
B | ASP163 |
B | GLN164 |
B | GLY215 |
B | UDP301 |
B | EDO304 |
B | HOH413 |
site_id | AC6 |
Number of Residues | 2 |
Details | binding site for residue EDO B 304 |
Chain | Residue |
B | UDP301 |
B | 2PE303 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:22160680, ECO:0000269|PubMed:30356213, ECO:0007744|PDB:3RMW, ECO:0007744|PDB:3T7O |
Chain | Residue | Details |
A | LEU9 | |
B | LEU9 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:22160680, ECO:0007744|PDB:3T7M, ECO:0007744|PDB:3T7N, ECO:0007744|PDB:3T7O, ECO:0007744|PDB:3U2U, ECO:0007744|PDB:3U2V, ECO:0007744|PDB:3U2W, ECO:0007744|PDB:3U2X |
Chain | Residue | Details |
A | ARG77 | |
B | ARG77 |
site_id | SWS_FT_FI3 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000269|PubMed:22160680, ECO:0000269|PubMed:30356213, ECO:0007744|PDB:3QVB, ECO:0007744|PDB:3RMV, ECO:0007744|PDB:3RMW, ECO:0007744|PDB:3T7M, ECO:0007744|PDB:3T7N, ECO:0007744|PDB:3T7O, ECO:0007744|PDB:3U2T, ECO:0007744|PDB:3U2U, ECO:0007744|PDB:3U2V, ECO:0007744|PDB:3U2W, ECO:0007744|PDB:3U2X |
Chain | Residue | Details |
A | ASP102 | |
A | ASP104 | |
A | HIS212 | |
B | ASP102 | |
B | ASP104 | |
B | HIS212 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:22160680, ECO:0007744|PDB:3RMW, ECO:0007744|PDB:3T7O |
Chain | Residue | Details |
A | ASN133 | |
A | ASP160 | |
B | ASN133 | |
B | ASP160 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | SITE: Important for catalytic activity => ECO:0000250|UniProtKB:P13280 |
Chain | Residue | Details |
A | LYS86 | |
B | LYS86 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | MOD_RES: N-acetylthreonine => ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895 |
Chain | Residue | Details |
A | THR2 | |
B | THR2 |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P13280 |
Chain | Residue | Details |
A | SER44 | |
B | SER44 |
site_id | SWS_FT_FI8 |
Number of Residues | 2 |
Details | CARBOHYD: O-linked (Glc...) tyrosine => ECO:0000269|PubMed:22160680, ECO:0000269|PubMed:30356213, ECO:0007744|PDB:3U2U, ECO:0007744|PDB:3U2V |
Chain | Residue | Details |
A | PHI195 | |
B | PHI195 |