7LUY
Crystal Structure of guanylate kinase from Bartonella henselae str. Houston-1
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004385 | molecular_function | guanylate kinase activity |
A | 0005524 | molecular_function | ATP binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0006163 | biological_process | purine nucleotide metabolic process |
A | 0016301 | molecular_function | kinase activity |
A | 0046037 | biological_process | GMP metabolic process |
A | 0046710 | biological_process | GDP metabolic process |
B | 0004385 | molecular_function | guanylate kinase activity |
B | 0005524 | molecular_function | ATP binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0006163 | biological_process | purine nucleotide metabolic process |
B | 0016301 | molecular_function | kinase activity |
B | 0046037 | biological_process | GMP metabolic process |
B | 0046710 | biological_process | GDP metabolic process |
C | 0004385 | molecular_function | guanylate kinase activity |
C | 0005524 | molecular_function | ATP binding |
C | 0005737 | cellular_component | cytoplasm |
C | 0005829 | cellular_component | cytosol |
C | 0006163 | biological_process | purine nucleotide metabolic process |
C | 0016301 | molecular_function | kinase activity |
C | 0046037 | biological_process | GMP metabolic process |
C | 0046710 | biological_process | GDP metabolic process |
D | 0004385 | molecular_function | guanylate kinase activity |
D | 0005524 | molecular_function | ATP binding |
D | 0005737 | cellular_component | cytoplasm |
D | 0005829 | cellular_component | cytosol |
D | 0006163 | biological_process | purine nucleotide metabolic process |
D | 0016301 | molecular_function | kinase activity |
D | 0046037 | biological_process | GMP metabolic process |
D | 0046710 | biological_process | GDP metabolic process |
E | 0004385 | molecular_function | guanylate kinase activity |
E | 0005524 | molecular_function | ATP binding |
E | 0005737 | cellular_component | cytoplasm |
E | 0005829 | cellular_component | cytosol |
E | 0006163 | biological_process | purine nucleotide metabolic process |
E | 0016301 | molecular_function | kinase activity |
E | 0046037 | biological_process | GMP metabolic process |
E | 0046710 | biological_process | GDP metabolic process |
F | 0004385 | molecular_function | guanylate kinase activity |
F | 0005524 | molecular_function | ATP binding |
F | 0005737 | cellular_component | cytoplasm |
F | 0005829 | cellular_component | cytosol |
F | 0006163 | biological_process | purine nucleotide metabolic process |
F | 0016301 | molecular_function | kinase activity |
F | 0046037 | biological_process | GMP metabolic process |
F | 0046710 | biological_process | GDP metabolic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | binding site for residue SO4 A 301 |
Chain | Residue |
A | GLY29 |
A | ALA30 |
A | GLY31 |
A | LYS32 |
A | SER33 |
A | HOH424 |
site_id | AC2 |
Number of Residues | 5 |
Details | binding site for residue SO4 A 302 |
Chain | Residue |
A | HOH430 |
A | HOH454 |
A | LYS121 |
A | HIS172 |
A | SER175 |
site_id | AC3 |
Number of Residues | 4 |
Details | binding site for residue EDO A 303 |
Chain | Residue |
A | LYS75 |
A | ARG78 |
B | ARG78 |
B | TRP86 |
site_id | AC4 |
Number of Residues | 4 |
Details | binding site for residue SO4 A 304 |
Chain | Residue |
A | ARG57 |
A | HIS90 |
A | ARG162 |
A | HOH414 |
site_id | AC5 |
Number of Residues | 6 |
Details | binding site for residue SO4 B 301 |
Chain | Residue |
B | LYS121 |
B | HIS172 |
B | SER175 |
B | HOH426 |
B | HOH438 |
B | HOH459 |
site_id | AC6 |
Number of Residues | 3 |
Details | binding site for residue EDO B 302 |
Chain | Residue |
A | ARG78 |
A | TRP86 |
B | ARG78 |
site_id | AC7 |
Number of Residues | 2 |
Details | binding site for residue EDO B 303 |
Chain | Residue |
B | HIS90 |
B | ASN165 |
site_id | AC8 |
Number of Residues | 4 |
Details | binding site for residue SO4 C 301 |
Chain | Residue |
C | LYS121 |
C | GLN171 |
C | HIS172 |
C | SER175 |
site_id | AC9 |
Number of Residues | 6 |
Details | binding site for residue SO4 D 301 |
Chain | Residue |
D | GLY29 |
D | ALA30 |
D | GLY31 |
D | LYS32 |
D | SER33 |
D | HOH405 |
site_id | AD1 |
Number of Residues | 5 |
Details | binding site for residue SO4 D 302 |
Chain | Residue |
D | LYS121 |
D | HIS172 |
D | ARG174 |
D | SER175 |
D | HOH415 |
site_id | AD2 |
Number of Residues | 3 |
Details | binding site for residue EDO D 303 |
Chain | Residue |
C | ASN214 |
D | TRP173 |
D | ARG174 |
site_id | AD3 |
Number of Residues | 1 |
Details | binding site for residue EDO D 304 |
Chain | Residue |
D | LYS121 |
site_id | AD4 |
Number of Residues | 7 |
Details | binding site for residue SO4 E 301 |
Chain | Residue |
E | GLY29 |
E | ALA30 |
E | GLY31 |
E | LYS32 |
E | SER33 |
E | ARG147 |
E | ARG151 |
site_id | AD5 |
Number of Residues | 5 |
Details | binding site for residue SO4 E 302 |
Chain | Residue |
C | ARG76 |
E | TYR117 |
E | HIS172 |
E | SER175 |
E | HOH420 |
site_id | AD6 |
Number of Residues | 3 |
Details | binding site for residue EDO E 303 |
Chain | Residue |
E | THR34 |
E | ARG147 |
E | ARG150 |
site_id | AD7 |
Number of Residues | 3 |
Details | binding site for residue EDO E 304 |
Chain | Residue |
E | ASP154 |
E | SER155 |
E | GLN156 |
site_id | AD8 |
Number of Residues | 4 |
Details | binding site for residue EDO E 305 |
Chain | Residue |
B | ASN214 |
E | GLN171 |
E | TRP173 |
E | ARG174 |
site_id | AD9 |
Number of Residues | 5 |
Details | binding site for residue EDO E 306 |
Chain | Residue |
E | THR131 |
E | ASP177 |
E | GLU199 |
E | LYS202 |
E | HOH408 |
site_id | AE1 |
Number of Residues | 4 |
Details | binding site for residue SO4 F 301 |
Chain | Residue |
D | ARG76 |
F | TYR117 |
F | HIS172 |
F | SER175 |
Functional Information from PROSITE/UniProt
site_id | PS00856 |
Number of Residues | 18 |
Details | GUANYLATE_KINASE_1 Guanylate kinase-like signature. TTRqkRpsEvdGlhYhFI |
Chain | Residue | Details |
A | THR52-ILE69 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00328 |
Chain | Residue | Details |
A | SER26 | |
B | SER26 | |
C | SER26 | |
D | SER26 | |
E | SER26 | |
F | SER26 |