2YID
Crystal structure of the SucA domain of Mycobacterium smegmatis alpha- ketoglutarate decarboxylase in complex with the enamine-ThDP intermediate
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 | 29 |
Details | BINDING SITE FOR RESIDUE TD7 A 2001 |
Chain | Residue |
A | PHE506 |
A | ASP645 |
A | ALA646 |
A | ALA647 |
A | GLN651 |
A | ASN678 |
A | ILE680 |
A | GLY681 |
A | HIS747 |
A | MG2002 |
A | HOH3022 |
A | HIS539 |
A | HOH3024 |
A | HOH3046 |
A | HOH3047 |
A | HOH3203 |
B | GLN901 |
B | LEU950 |
B | GLU952 |
B | GLN976 |
B | PHE980 |
B | HIS1020 |
A | ARG540 |
A | TYR578 |
A | HIS579 |
A | SER604 |
A | HIS605 |
A | LEU606 |
A | GLY644 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG A 2002 |
Chain | Residue |
A | ASP645 |
A | ASN678 |
A | ILE680 |
A | TD72001 |
A | HOH3047 |
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 | HOH3153 |
A | HOH3154 |
site_id | AC4 |
Number of Residues | 28 |
Details | BINDING SITE FOR RESIDUE TD7 B 2001 |
Chain | Residue |
A | GLN901 |
A | LEU950 |
A | GLU952 |
A | GLN976 |
A | PHE980 |
A | HIS1020 |
B | PHE506 |
B | HIS539 |
B | ARG540 |
B | TYR578 |
B | HIS579 |
B | SER604 |
B | HIS605 |
B | LEU606 |
B | GLY644 |
B | ASP645 |
B | ALA646 |
B | ALA647 |
B | ASN678 |
B | ILE680 |
B | GLY681 |
B | HIS747 |
B | MG2002 |
B | HOH3027 |
B | HOH3028 |
B | HOH3049 |
B | HOH3050 |
B | HOH3065 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG B 2002 |
Chain | Residue |
B | ASP645 |
B | ASN678 |
B | ILE680 |
B | TD72001 |
B | HOH3050 |
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 | HOH3127 |
B | HOH3128 |
site_id | AC7 |
Number of Residues | 28 |
Details | BINDING SITE FOR RESIDUE TD7 C 2001 |
Chain | Residue |
C | HOH3061 |
C | HOH3062 |
D | GLN901 |
D | LEU950 |
D | GLU952 |
D | GLN976 |
D | PHE980 |
D | HIS1020 |
C | HIS539 |
C | ARG540 |
C | TYR578 |
C | HIS579 |
C | SER604 |
C | HIS605 |
C | LEU606 |
C | GLY644 |
C | ASP645 |
C | ALA646 |
C | ALA647 |
C | GLN651 |
C | ASN678 |
C | ILE680 |
C | GLY681 |
C | HIS747 |
C | MG2002 |
C | HOH3031 |
C | HOH3032 |
C | HOH3034 |
site_id | AC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG C 2002 |
Chain | Residue |
C | ASP645 |
C | ASN678 |
C | ILE680 |
C | TD72001 |
C | HOH3062 |
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 | HOH3177 |
C | HOH3178 |
site_id | BC1 |
Number of Residues | 28 |
Details | BINDING SITE FOR RESIDUE TD7 D 2001 |
Chain | Residue |
C | GLN901 |
C | LEU950 |
C | GLU952 |
C | GLN976 |
C | PHE980 |
C | HIS1020 |
D | HIS539 |
D | ARG540 |
D | TYR578 |
D | HIS579 |
D | SER604 |
D | HIS605 |
D | LEU606 |
D | GLY644 |
D | ASP645 |
D | ALA646 |
D | ALA647 |
D | GLN651 |
D | ASN678 |
D | ILE680 |
D | GLY681 |
D | HIS747 |
D | MG2002 |
D | HOH3018 |
D | HOH3019 |
D | HOH3021 |
D | HOH3037 |
D | HOH3038 |
site_id | BC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG D 2002 |
Chain | Residue |
D | ASP645 |
D | ASN678 |
D | ILE680 |
D | TD72001 |
D | HOH3038 |
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 | HOH3100 |
D | HOH3101 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 60 |
Details | BINDING: BINDING => ECO:0000269|PubMed:21867916, ECO:0007744|PDB:2XTA |
Chain | Residue | Details |
A | ARG540 | |
A | ARG1054 | |
A | LYS1089 | |
A | SER1092 | |
A | GLN1142 | |
A | ARG1149 | |
A | ARG1150 | |
B | ARG540 | |
B | SER604 | |
B | LEU606 | |
B | ASP645 | |
A | SER604 | |
B | ALA646 | |
B | ALA647 | |
B | ASN678 | |
B | ILE680 | |
B | THR1038 | |
B | ARG1054 | |
B | LYS1089 | |
B | SER1092 | |
B | GLN1142 | |
B | ARG1149 | |
A | LEU606 | |
B | ARG1150 | |
C | ARG540 | |
C | SER604 | |
C | LEU606 | |
C | ASP645 | |
C | ALA646 | |
C | ALA647 | |
C | ASN678 | |
C | ILE680 | |
C | THR1038 | |
A | ASP645 | |
C | ARG1054 | |
C | LYS1089 | |
C | SER1092 | |
C | GLN1142 | |
C | ARG1149 | |
C | ARG1150 | |
D | ARG540 | |
D | SER604 | |
D | LEU606 | |
D | ASP645 | |
A | ALA646 | |
D | ALA646 | |
D | ALA647 | |
D | ASN678 | |
D | ILE680 | |
D | THR1038 | |
D | ARG1054 | |
D | LYS1089 | |
D | SER1092 | |
D | GLN1142 | |
D | ARG1149 | |
A | ALA647 | |
D | ARG1150 | |
A | ASN678 | |
A | ILE680 | |
A | THR1038 |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000305|PubMed:21867916, ECO:0007744|PDB:2Y0P |
Chain | Residue | Details |
A | HIS579 | |
A | HIS1020 | |
B | HIS579 | |
B | HIS1020 | |
C | HIS579 | |
C | HIS1020 | |
D | HIS579 | |
D | HIS1020 |