3ZHS
Crystal structure of the SucA domain of Mycobacterium smegmatis KGD, first post-decarboxylation intermediate from alpha-ketoglutarate
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 | 26 |
Details | BINDING SITE FOR RESIDUE TD6 A 2001 |
Chain | Residue |
A | ARG540 |
A | ILE680 |
A | GLY681 |
A | PHE682 |
A | HIS747 |
A | ASN748 |
A | MG2002 |
A | HOH3026 |
A | HOH3042 |
A | HOH3073 |
A | HOH3074 |
A | SER604 |
A | HOH3316 |
B | GLN901 |
B | LEU950 |
B | GLU952 |
B | GLN976 |
B | PHE980 |
B | HIS1020 |
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 | TD62001 |
A | HOH3074 |
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 | HOH3226 |
A | HOH3227 |
site_id | AC4 |
Number of Residues | 28 |
Details | BINDING SITE FOR RESIDUE TD6 B 2001 |
Chain | Residue |
A | GLN901 |
A | LEU950 |
A | GLU952 |
A | GLN976 |
A | PHE980 |
A | HIS1020 |
B | ARG505 |
B | ARG540 |
B | SER604 |
B | HIS605 |
B | LEU606 |
B | GLY644 |
B | ASP645 |
B | ALA646 |
B | ALA647 |
B | ASN678 |
B | ILE680 |
B | GLY681 |
B | PHE682 |
B | HIS747 |
B | ASN748 |
B | MG2002 |
B | HOH3037 |
B | HOH3038 |
B | HOH3039 |
B | HOH3069 |
B | HOH3070 |
B | HOH3241 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG B 2002 |
Chain | Residue |
B | ASP645 |
B | ASN678 |
B | ILE680 |
B | TD62001 |
B | HOH3070 |
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 | HOH3174 |
B | HOH3175 |
site_id | AC7 |
Number of Residues | 28 |
Details | BINDING SITE FOR RESIDUE TD6 C 2001 |
Chain | Residue |
D | LEU950 |
D | GLU952 |
D | GLN976 |
D | PHE980 |
D | HIS1020 |
C | ARG505 |
C | ARG540 |
C | SER604 |
C | HIS605 |
C | LEU606 |
C | GLY644 |
C | ASP645 |
C | ALA646 |
C | ALA647 |
C | ASN678 |
C | ILE680 |
C | GLY681 |
C | PHE682 |
C | HIS747 |
C | ASN748 |
C | MG2002 |
C | HOH3022 |
C | HOH3034 |
C | HOH3036 |
C | HOH3063 |
C | HOH3064 |
C | HOH3272 |
D | GLN901 |
site_id | AC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG C 2002 |
Chain | Residue |
C | ASP645 |
C | ASN678 |
C | ILE680 |
C | TD62001 |
C | HOH3064 |
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 | HOH3203 |
C | HOH3204 |
site_id | BC1 |
Number of Residues | 26 |
Details | BINDING SITE FOR RESIDUE TD6 D 2001 |
Chain | Residue |
C | GLN901 |
C | LEU950 |
C | GLU952 |
C | GLN976 |
C | PHE980 |
C | HIS1020 |
D | ARG540 |
D | SER604 |
D | HIS605 |
D | LEU606 |
D | GLY644 |
D | ASP645 |
D | ALA646 |
D | ALA647 |
D | ASN678 |
D | ILE680 |
D | GLY681 |
D | PHE682 |
D | HIS747 |
D | ASN748 |
D | MG2002 |
D | HOH3033 |
D | HOH3034 |
D | HOH3060 |
D | HOH3061 |
D | HOH3211 |
site_id | BC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG D 2002 |
Chain | Residue |
D | ASP645 |
D | ASN678 |
D | ILE680 |
D | TD62001 |
D | HOH3061 |
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 | HOH3163 |
D | HOH3164 |
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 |