1DJL
THE CRYSTAL STRUCTURE OF HUMAN TRANSHYDROGENASE DOMAIN III WITH BOUND NADP
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1138 |
| Chain | Residue |
| A | HOH6 |
| A | ARG1000 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 B 2138 |
| Chain | Residue |
| B | HOH43 |
| B | ARG1000 |
| site_id | AC3 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE NAP A 1136 |
| Chain | Residue |
| A | GLY889 |
| A | TYR890 |
| A | GLY891 |
| A | ALA895 |
| A | VAL922 |
| A | ALA923 |
| A | GLY924 |
| A | ARG925 |
| A | MET926 |
| A | PRO927 |
| A | GLY964 |
| A | ALA965 |
| A | ASN966 |
| A | ASP967 |
| A | THR968 |
| A | ALA982 |
| A | GLY983 |
| A | MET984 |
| A | LYS999 |
| A | ARG1000 |
| A | SER1001 |
| A | VAL1004 |
| A | GLY1005 |
| A | TYR1006 |
| A | ASP1025 |
| A | ALA1026 |
| A | GOL1137 |
| A | HOH6 |
| A | HOH9 |
| A | HOH54 |
| A | HOH62 |
| A | HOH80 |
| site_id | AC4 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE NAP B 2136 |
| Chain | Residue |
| B | HOH31 |
| B | HOH40 |
| B | HOH43 |
| B | GLY889 |
| B | TYR890 |
| B | GLY891 |
| B | ALA895 |
| B | VAL922 |
| B | ALA923 |
| B | GLY924 |
| B | ARG925 |
| B | MET926 |
| B | PRO927 |
| B | GLY964 |
| B | ALA965 |
| B | ASN966 |
| B | ASP967 |
| B | THR968 |
| B | LYS999 |
| B | ARG1000 |
| B | SER1001 |
| B | VAL1004 |
| B | GLY1005 |
| B | TYR1006 |
| B | GLY1024 |
| B | ASP1025 |
| B | ALA1026 |
| B | GOL2137 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 1137 |
| Chain | Residue |
| A | HIS920 |
| A | VAL922 |
| A | ASP967 |
| A | ILE981 |
| A | PRO985 |
| A | VAL986 |
| A | NAP1136 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B 2137 |
| Chain | Residue |
| B | HIS920 |
| B | ASP967 |
| B | ILE981 |
| B | MET984 |
| B | VAL986 |
| B | NAP2136 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 36 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10673423","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12791694","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15323555","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1DJL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1PT9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1U31","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10673423","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15323555","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1DJL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1U31","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q61941","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | a catalytic site defined by CSA, PubMed 10673423 |
| Chain | Residue | Details |
| A | TYR890 | |
| A | TYR1006 | |
| A | ARG925 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | a catalytic site defined by CSA, PubMed 10673423 |
| Chain | Residue | Details |
| B | TYR890 | |
| A | TYR1006 | |
| B | ARG925 |
| site_id | MCSA1 |
| Number of Residues | 3 |
| Details | M-CSA 496 |
| Chain | Residue | Details |
| A | TYR890 | electrostatic stabiliser |
| A | ARG925 | electrostatic stabiliser |
| A | TYR1006 | electrostatic stabiliser |
| site_id | MCSA2 |
| Number of Residues | 3 |
| Details | M-CSA 496 |
| Chain | Residue | Details |
| B | TYR890 | electrostatic stabiliser |
| B | ARG925 | electrostatic stabiliser |
| B | TYR1006 | electrostatic stabiliser |
