9FKF
Crystal structure of human Glucose-6-phosphate isomerase with phosphoenol pyruvate ligand
Functional Information from PROSITE/UniProt
| site_id | PS00174 |
| Number of Residues | 18 |
| Details | P_GLUCOSE_ISOMERASE_2 Phosphoglucose isomerase signature 2. GiIWdinsFDQwGVElgK |
| Chain | Residue | Details |
| A | GLY502-LYS519 |
| site_id | PS00765 |
| Number of Residues | 14 |
| Details | P_GLUCOSE_ISOMERASE_1 Phosphoglucose isomerase signature 1. DwVGGRYSLwSAIG |
| Chain | Residue | Details |
| A | ASP268-GLY281 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton donor => ECO:0000269|PubMed:11371164, ECO:0000269|PubMed:12573240, ECO:0000269|PubMed:12777791 |
| Chain | Residue | Details |
| A | GLU358 | |
| B | GLU358 | |
| C | GLU358 | |
| D | GLU358 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | ACT_SITE: ACT_SITE => ECO:0000269|PubMed:11371164, ECO:0000269|PubMed:12573240, ECO:0000269|PubMed:12777791 |
| Chain | Residue | Details |
| A | HIS389 | |
| A | LYS519 | |
| B | HIS389 | |
| B | LYS519 | |
| C | HIS389 | |
| C | LYS519 | |
| D | HIS389 | |
| D | LYS519 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 24 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P06745 |
| Chain | Residue | Details |
| A | GLY159 | |
| B | GLU358 | |
| B | HIS389 | |
| B | LYS519 | |
| C | GLY159 | |
| C | SER210 | |
| C | GLN354 | |
| C | GLU358 | |
| C | HIS389 | |
| C | LYS519 | |
| D | GLY159 | |
| A | SER210 | |
| D | SER210 | |
| D | GLN354 | |
| D | GLU358 | |
| D | HIS389 | |
| D | LYS519 | |
| A | GLN354 | |
| A | GLU358 | |
| A | HIS389 | |
| A | LYS519 | |
| B | GLY159 | |
| B | SER210 | |
| B | GLN354 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | MOD_RES: N-acetylalanine => ECO:0000269|Ref.8, ECO:0007744|PubMed:19413330 |
| Chain | Residue | Details |
| A | ALA2 | |
| B | ALA2 | |
| C | ALA2 | |
| D | ALA2 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 8 |
| Details | MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861 |
| Chain | Residue | Details |
| A | LYS12 | |
| A | LYS142 | |
| B | LYS12 | |
| B | LYS142 | |
| C | LYS12 | |
| C | LYS142 | |
| D | LYS12 | |
| D | LYS142 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-(2-hydroxyisobutyryl)lysine => ECO:0000269|PubMed:29775581 |
| Chain | Residue | Details |
| A | LYS34 | |
| B | LYS34 | |
| C | LYS34 | |
| D | LYS34 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 8 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| A | SER107 | |
| A | SER455 | |
| B | SER107 | |
| B | SER455 | |
| C | SER107 | |
| C | SER455 | |
| D | SER107 | |
| D | SER455 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569 |
| Chain | Residue | Details |
| A | THR109 | |
| B | THR109 | |
| C | THR109 | |
| D | THR109 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine; by CK2 => ECO:0000269|PubMed:11004567, ECO:0000269|PubMed:15637053 |
| Chain | Residue | Details |
| A | SER185 | |
| B | SER185 | |
| C | SER185 | |
| D | SER185 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q6P6V0 |
| Chain | Residue | Details |
| A | THR250 | |
| B | THR250 | |
| C | THR250 | |
| D | THR250 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P06745 |
| Chain | Residue | Details |
| A | LYS454 | |
| B | LYS454 | |
| C | LYS454 | |
| D | LYS454 |
