5TXR
Structure of ALAS from S. cerevisiae non-covalently bound to PLP cofactor
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003870 | molecular_function | 5-aminolevulinate synthase activity |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005759 | cellular_component | mitochondrial matrix |
| A | 0006782 | biological_process | protoporphyrinogen IX biosynthetic process |
| A | 0006783 | biological_process | heme biosynthetic process |
| A | 0009058 | biological_process | biosynthetic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016746 | molecular_function | acyltransferase activity |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0033014 | biological_process | tetrapyrrole biosynthetic process |
| A | 1902117 | biological_process | positive regulation of organelle assembly |
| B | 0003870 | molecular_function | 5-aminolevulinate synthase activity |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0005759 | cellular_component | mitochondrial matrix |
| B | 0006782 | biological_process | protoporphyrinogen IX biosynthetic process |
| B | 0006783 | biological_process | heme biosynthetic process |
| B | 0009058 | biological_process | biosynthetic process |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016746 | molecular_function | acyltransferase activity |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0033014 | biological_process | tetrapyrrole biosynthetic process |
| B | 1902117 | biological_process | positive regulation of organelle assembly |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | binding site for residue FMT B 601 |
| Chain | Residue |
| B | ALA258 |
| B | ARG459 |
| B | HOH873 |
| B | HOH876 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue FMT B 602 |
| Chain | Residue |
| A | THR150 |
| A | ASN152 |
| A | HOH813 |
| B | ARG91 |
| B | THR452 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | binding site for residue FMT B 603 |
| Chain | Residue |
| B | LYS128 |
| B | HOH840 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue FMT B 604 |
| Chain | Residue |
| B | GLU131 |
| B | ARG382 |
| B | TYR383 |
| B | HOH716 |
| site_id | AC5 |
| Number of Residues | 18 |
| Details | binding site for residue PLP B 605 |
| Chain | Residue |
| A | THR366 |
| A | THR367 |
| B | SER181 |
| B | CYS182 |
| B | TYR183 |
| B | ASN186 |
| B | HIS209 |
| B | SER211 |
| B | GLU252 |
| B | ASP281 |
| B | VAL283 |
| B | HIS284 |
| B | THR334 |
| B | LYS337 |
| B | GLY343 |
| B | HOH730 |
| B | HOH850 |
| B | HOH964 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | binding site for residue GOL A 601 |
| Chain | Residue |
| A | ASP329 |
| A | SER349 |
| A | HOH751 |
| A | HOH945 |
| A | HOH958 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for residue K A 602 |
| Chain | Residue |
| A | SER304 |
| A | THR315 |
| A | ASN316 |
| A | HOH1010 |
| A | HOH1044 |
| A | HOH1066 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | binding site for residue FMT A 603 |
| Chain | Residue |
| A | LEU207 |
| A | TYR255 |
| A | MET257 |
| A | ALA258 |
| A | GLY259 |
| A | SER260 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | binding site for residue FMT A 604 |
| Chain | Residue |
| A | ALA307 |
| A | ASN529 |
| A | HOH702 |
| site_id | AD1 |
| Number of Residues | 4 |
| Details | binding site for residue FMT A 605 |
| Chain | Residue |
| A | LYS217 |
| A | HIS218 |
| A | HOH868 |
| B | HIS218 |
| site_id | AD2 |
| Number of Residues | 8 |
| Details | binding site for residue FMT A 606 |
| Chain | Residue |
| A | GLU265 |
| A | CYS300 |
| A | ASP301 |
| A | ASP317 |
| A | LYS318 |
| A | HOH703 |
| A | HOH704 |
| A | HOH925 |
| site_id | AD3 |
| Number of Residues | 6 |
| Details | binding site for residue FMT A 607 |
| Chain | Residue |
| A | SER204 |
| A | ASP205 |
| A | ILE225 |
| A | HOH706 |
| A | HOH709 |
| A | HOH788 |
| site_id | AD4 |
| Number of Residues | 6 |
| Details | binding site for residue FMT A 608 |
| Chain | Residue |
| A | GLU252 |
| A | TYR255 |
| A | SER256 |
| A | HIS284 |
| A | PLP609 |
| A | HOH763 |
| site_id | AD5 |
| Number of Residues | 18 |
| Details | binding site for residue PLP A 609 |
| Chain | Residue |
| A | SER181 |
| A | CYS182 |
| A | TYR183 |
| A | ASN186 |
| A | HIS209 |
| A | SER211 |
| A | GLU252 |
| A | ASP281 |
| A | VAL283 |
| A | HIS284 |
| A | THR334 |
| A | LYS337 |
| A | GLY343 |
| A | FMT608 |
| A | HOH734 |
| A | HOH805 |
| B | THR366 |
| B | THR367 |
Functional Information from PROSITE/UniProt
| site_id | PS00599 |
| Number of Residues | 10 |
| Details | AA_TRANSFER_CLASS_2 Aminotransferases class-II pyridoxal-phosphate attachment site. TLGKSFGSVG |
| Chain | Residue | Details |
| B | THR334-GLY343 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"evidences":[{"source":"UniProtKB","id":"P18079","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P18079","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | Binding site: {"description":"in other chain","evidences":[{"source":"UniProtKB","id":"P18079","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"UniProtKB","id":"P18079","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
