3N1T
Crystal structure of the H101A mutant ecHint GMP complex
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0003824 | molecular_function | catalytic activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0016787 | molecular_function | hydrolase activity |
A | 0042803 | molecular_function | protein homodimerization activity |
A | 0043530 | molecular_function | adenosine 5'-monophosphoramidase activity |
A | 0055130 | biological_process | D-alanine catabolic process |
B | 0000166 | molecular_function | nucleotide binding |
B | 0003824 | molecular_function | catalytic activity |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0016787 | molecular_function | hydrolase activity |
B | 0042803 | molecular_function | protein homodimerization activity |
B | 0043530 | molecular_function | adenosine 5'-monophosphoramidase activity |
B | 0055130 | biological_process | D-alanine catabolic process |
E | 0000166 | molecular_function | nucleotide binding |
E | 0003824 | molecular_function | catalytic activity |
E | 0005737 | cellular_component | cytoplasm |
E | 0005829 | cellular_component | cytosol |
E | 0016787 | molecular_function | hydrolase activity |
E | 0042803 | molecular_function | protein homodimerization activity |
E | 0043530 | molecular_function | adenosine 5'-monophosphoramidase activity |
E | 0055130 | biological_process | D-alanine catabolic process |
F | 0000166 | molecular_function | nucleotide binding |
F | 0003824 | molecular_function | catalytic activity |
F | 0005737 | cellular_component | cytoplasm |
F | 0005829 | cellular_component | cytosol |
F | 0016787 | molecular_function | hydrolase activity |
F | 0042803 | molecular_function | protein homodimerization activity |
F | 0043530 | molecular_function | adenosine 5'-monophosphoramidase activity |
F | 0055130 | biological_process | D-alanine catabolic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE 5GP A 200 |
Chain | Residue |
A | ILE6 |
A | GLU96 |
A | VAL97 |
A | HIS103 |
A | HOH127 |
A | HOH132 |
A | HOH179 |
A | HOH184 |
A | ILE10 |
A | ARG30 |
A | ASP31 |
A | ILE32 |
A | SER33 |
A | LEU41 |
A | ASN88 |
A | GLN95 |
site_id | AC2 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE 5GP B 200 |
Chain | Residue |
A | ARG13 |
A | HOH183 |
B | ILE6 |
B | PHE29 |
B | ARG30 |
B | ASP31 |
B | ILE32 |
B | LEU41 |
B | ASN88 |
B | GLN95 |
B | GLU96 |
B | VAL97 |
B | HIS103 |
B | HOH121 |
B | HOH125 |
B | HOH134 |
B | HOH141 |
site_id | AC3 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE 5GP E 200 |
Chain | Residue |
E | ILE6 |
E | ARG30 |
E | ASP31 |
E | ILE32 |
E | SER33 |
E | LEU41 |
E | ASN88 |
E | GLN95 |
E | GLU96 |
E | VAL97 |
E | HIS103 |
E | HOH121 |
E | HOH140 |
E | HOH145 |
E | HOH147 |
E | HOH164 |
F | ARG13 |
F | HOH185 |
site_id | AC4 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE 5GP F 200 |
Chain | Residue |
F | ILE6 |
F | PHE7 |
F | ILE10 |
F | ARG30 |
F | ASP31 |
F | ILE32 |
F | LEU41 |
F | ASN88 |
F | GLN95 |
F | GLU96 |
F | VAL97 |
F | HIS103 |
F | HOH123 |
F | HOH129 |
F | HOH133 |
F | HOH156 |
F | HOH161 |
F | HOH164 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: Tele-AMP-histidine intermediate => ECO:0000269|PubMed:15703176, ECO:0000269|PubMed:20934431 |
Chain | Residue | Details |
A | ALA101 | |
B | ALA101 | |
E | ALA101 | |
F | ALA101 |
site_id | SWS_FT_FI2 |
Number of Residues | 16 |
Details | BINDING: BINDING => ECO:0000269|PubMed:20934431, ECO:0007744|PDB:3N1S |
Chain | Residue | Details |
A | ARG30 | |
E | ASN88 | |
E | GLU96 | |
E | ALA101 | |
F | ARG30 | |
F | ASN88 | |
F | GLU96 | |
F | ALA101 | |
A | ASN88 | |
A | GLU96 | |
A | ALA101 | |
B | ARG30 | |
B | ASN88 | |
B | GLU96 | |
B | ALA101 | |
E | ARG30 |