3ZHQ
Crystal structure of the H747A mutant of the SucA domain of Mycobacterium smegmatis KGD
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0016624 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor |
| A | 0030976 | molecular_function | thiamine pyrophosphate binding |
| B | 0016624 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor |
| B | 0030976 | molecular_function | thiamine pyrophosphate binding |
| C | 0016624 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor |
| C | 0030976 | molecular_function | thiamine pyrophosphate binding |
| D | 0016624 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor |
| D | 0030976 | molecular_function | thiamine pyrophosphate binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE TPP A 2001 |
| Chain | Residue |
| A | ARG540 |
| A | ILE680 |
| A | GLY681 |
| A | MG2002 |
| A | HOH3031 |
| A | HOH3051 |
| A | HOH3052 |
| A | HOH3071 |
| A | HOH3196 |
| B | GLN901 |
| B | LEU950 |
| A | SER604 |
| B | GLU952 |
| B | GLN976 |
| B | PHE980 |
| A | HIS605 |
| A | LEU606 |
| A | GLY644 |
| A | ASP645 |
| A | ALA646 |
| A | ALA647 |
| A | ASN678 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 2002 |
| Chain | Residue |
| A | ASP645 |
| A | ASN678 |
| A | ILE680 |
| A | TPP2001 |
| A | HOH3052 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 2003 |
| Chain | Residue |
| A | ASP1004 |
| A | HIS1055 |
| A | ASP1058 |
| A | ILE1060 |
| A | HOH3140 |
| A | HOH3141 |
| site_id | AC4 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE TPP B 2001 |
| Chain | Residue |
| A | GLN901 |
| A | LEU950 |
| A | GLU952 |
| A | GLN976 |
| A | PHE980 |
| B | ARG540 |
| B | SER604 |
| B | HIS605 |
| B | LEU606 |
| B | GLY644 |
| B | ASP645 |
| B | ALA646 |
| B | ALA647 |
| B | ASN678 |
| B | ILE680 |
| B | GLY681 |
| B | MG2002 |
| B | HOH3040 |
| B | HOH3041 |
| B | HOH3056 |
| B | HOH3057 |
| B | HOH3154 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 2002 |
| Chain | Residue |
| B | ASP645 |
| B | ASN678 |
| B | ILE680 |
| B | TPP2001 |
| B | HOH3041 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA B 2003 |
| Chain | Residue |
| B | ASP1004 |
| B | HIS1055 |
| B | ASP1058 |
| B | ILE1060 |
| B | HOH3106 |
| B | HOH3107 |
| site_id | AC7 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE TPP C 2001 |
| Chain | Residue |
| C | ARG540 |
| C | SER604 |
| C | HIS605 |
| C | LEU606 |
| C | GLY644 |
| C | ASP645 |
| C | ALA646 |
| C | ALA647 |
| C | ASN678 |
| C | ILE680 |
| C | GLY681 |
| C | MG2002 |
| C | HOH3041 |
| C | HOH3056 |
| C | HOH3164 |
| D | GLN901 |
| D | LEU950 |
| D | GLU952 |
| D | GLN976 |
| D | PHE980 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG C 2002 |
| Chain | Residue |
| C | ASP645 |
| C | ASN678 |
| C | ILE680 |
| C | TPP2001 |
| C | HOH3041 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA C 2003 |
| Chain | Residue |
| C | ASP1004 |
| C | HIS1055 |
| C | ASP1058 |
| C | ILE1060 |
| C | HOH3120 |
| C | HOH3121 |
| site_id | BC1 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE TPP D 2001 |
| Chain | Residue |
| C | GLU952 |
| C | GLN976 |
| C | PHE980 |
| D | ARG540 |
| D | SER604 |
| D | HIS605 |
| D | LEU606 |
| D | GLY644 |
| D | ASP645 |
| D | ALA646 |
| D | ALA647 |
| D | ASN678 |
| D | ILE680 |
| D | GLY681 |
| D | MG2002 |
| D | HOH3020 |
| D | HOH3043 |
| D | HOH3044 |
| D | HOH3059 |
| D | HOH3127 |
| C | GLN901 |
| C | LEU950 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG D 2002 |
| Chain | Residue |
| D | ASP645 |
| D | ASN678 |
| D | ILE680 |
| D | TPP2001 |
| D | HOH3044 |
| site_id | BC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA D 2003 |
| Chain | Residue |
| D | ASP1004 |
| D | HIS1055 |
| D | ASP1058 |
| D | ILE1060 |
| D | HOH3093 |
| D | HOH3094 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 60 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"21867916","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2XTA","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"21867916","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"2Y0P","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 62 |
| Details | Coiled coil: {"evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
