3VOS
Crystal structure of Aspartate semialdehyde dehydrogenase Complexed With glycerol and sulfate From Mycobacterium tuberculosis H37Rv
Replaces: 3LLGReplaces: 3KUBFunctional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004073 | molecular_function | aspartate-semialdehyde dehydrogenase activity |
A | 0005515 | molecular_function | protein binding |
A | 0005886 | cellular_component | plasma membrane |
A | 0006520 | biological_process | amino acid metabolic process |
A | 0008652 | biological_process | amino acid biosynthetic process |
A | 0009085 | biological_process | lysine biosynthetic process |
A | 0009086 | biological_process | methionine biosynthetic process |
A | 0009088 | biological_process | threonine biosynthetic process |
A | 0009089 | biological_process | lysine biosynthetic process via diaminopimelate |
A | 0009097 | biological_process | isoleucine biosynthetic process |
A | 0009274 | cellular_component | peptidoglycan-based cell wall |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
A | 0019877 | biological_process | diaminopimelate biosynthetic process |
A | 0046983 | molecular_function | protein dimerization activity |
A | 0050661 | molecular_function | NADP binding |
A | 0051287 | molecular_function | NAD binding |
A | 0071266 | biological_process | 'de novo' L-methionine biosynthetic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GOL A 401 |
Chain | Residue |
A | CYS130 |
A | GLN157 |
A | GLY161 |
A | GLU224 |
A | ARG249 |
A | HIS256 |
A | SO4404 |
A | HOH825 |
A | HOH850 |
site_id | AC2 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE GOL A 402 |
Chain | Residue |
A | GLY188 |
A | GLY189 |
A | LEU191 |
A | PHE193 |
A | HOH613 |
A | HOH621 |
A | HOH680 |
A | HOH685 |
A | HOH722 |
A | HOH835 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL A 403 |
Chain | Residue |
A | ARG229 |
A | PHE230 |
A | ARG233 |
A | HOH682 |
A | HOH849 |
site_id | AC4 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SO4 A 404 |
Chain | Residue |
A | ARG99 |
A | ASN129 |
A | CYS130 |
A | LYS227 |
A | GOL401 |
A | HOH786 |
A | HOH851 |
A | HOH909 |
site_id | AC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 A 405 |
Chain | Residue |
A | GLU271 |
A | ARG274 |
A | HOH842 |
site_id | AC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 A 406 |
Chain | Residue |
A | HIS118 |
A | ARG120 |
A | HOH933 |
site_id | AC7 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 A 407 |
Chain | Residue |
A | ARG233 |
A | HOH662 |
A | HOH930 |
site_id | AC8 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SO4 A 408 |
Chain | Residue |
A | ARG43 |
A | GLU53 |
A | GLY73 |
A | SER74 |
A | HOH862 |
A | HOH869 |
A | HOH871 |
A | HOH898 |
site_id | AC9 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE SO4 A 409 |
Chain | Residue |
A | GLY12 |
A | GLN13 |
A | VAL14 |
A | ARG43 |
A | GLY163 |
A | LEU164 |
A | HOH629 |
A | HOH823 |
A | HOH876 |
A | HOH910 |
Functional Information from PROSITE/UniProt
site_id | PS01103 |
Number of Residues | 15 |
Details | ASD Aspartate-semialdehyde dehydrogenase signature. VSgtCvRVpvftGHS |
Chain | Residue | Details |
A | VAL243-SER257 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: Acyl-thioester intermediate => ECO:0000305|PubMed:22683789 |
Chain | Residue | Details |
A | CYS130 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | ACT_SITE: Proton acceptor => ECO:0000250 |
Chain | Residue | Details |
A | HIS256 |
site_id | SWS_FT_FI3 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | ARG39 | |
A | ARG99 | |
A | GLN157 | |
A | SER160 | |
A | LYS227 | |
A | ARG249 | |
A | ASN325 | |
A | THR11 |