4DU6
Crystal structure of GTP cyclohydrolase I from Yersinia pestis complexed with GTP
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003934 | molecular_function | GTP cyclohydrolase I activity |
A | 0005525 | molecular_function | GTP binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0006729 | biological_process | tetrahydrobiopterin biosynthetic process |
A | 0006730 | biological_process | one-carbon metabolic process |
A | 0008270 | molecular_function | zinc ion binding |
A | 0016787 | molecular_function | hydrolase activity |
A | 0046654 | biological_process | tetrahydrofolate biosynthetic process |
A | 0046872 | molecular_function | metal ion binding |
B | 0003934 | molecular_function | GTP cyclohydrolase I activity |
B | 0005525 | molecular_function | GTP binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0006729 | biological_process | tetrahydrobiopterin biosynthetic process |
B | 0006730 | biological_process | one-carbon metabolic process |
B | 0008270 | molecular_function | zinc ion binding |
B | 0016787 | molecular_function | hydrolase activity |
B | 0046654 | biological_process | tetrahydrofolate biosynthetic process |
B | 0046872 | molecular_function | metal ion binding |
C | 0003934 | molecular_function | GTP cyclohydrolase I activity |
C | 0005525 | molecular_function | GTP binding |
C | 0005737 | cellular_component | cytoplasm |
C | 0006729 | biological_process | tetrahydrobiopterin biosynthetic process |
C | 0006730 | biological_process | one-carbon metabolic process |
C | 0008270 | molecular_function | zinc ion binding |
C | 0016787 | molecular_function | hydrolase activity |
C | 0046654 | biological_process | tetrahydrofolate biosynthetic process |
C | 0046872 | molecular_function | metal ion binding |
D | 0003934 | molecular_function | GTP cyclohydrolase I activity |
D | 0005525 | molecular_function | GTP binding |
D | 0005737 | cellular_component | cytoplasm |
D | 0006729 | biological_process | tetrahydrobiopterin biosynthetic process |
D | 0006730 | biological_process | one-carbon metabolic process |
D | 0008270 | molecular_function | zinc ion binding |
D | 0016787 | molecular_function | hydrolase activity |
D | 0046654 | biological_process | tetrahydrofolate biosynthetic process |
D | 0046872 | molecular_function | metal ion binding |
E | 0003934 | molecular_function | GTP cyclohydrolase I activity |
E | 0005525 | molecular_function | GTP binding |
E | 0005737 | cellular_component | cytoplasm |
E | 0006729 | biological_process | tetrahydrobiopterin biosynthetic process |
E | 0006730 | biological_process | one-carbon metabolic process |
E | 0008270 | molecular_function | zinc ion binding |
E | 0016787 | molecular_function | hydrolase activity |
E | 0046654 | biological_process | tetrahydrofolate biosynthetic process |
E | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 20 |
Details | BINDING SITE FOR RESIDUE GTP A 301 |
Chain | Residue |
A | THR86 |
B | CYS109 |
B | HIS111 |
B | HIS112 |
B | VAL149 |
B | GLN150 |
B | GLU151 |
B | HIS178 |
B | CYS180 |
B | ARG184 |
B | CA305 |
A | VAL130 |
C | ARG64 |
A | ILE131 |
A | GLY132 |
A | LEU133 |
A | SER134 |
A | LYS135 |
A | ARG138 |
A | HOH426 |
site_id | AC2 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL A 302 |
Chain | Residue |
A | GLN155 |
A | LEU158 |
A | SER197 |
A | LEU198 |
A | LYS203 |
E | LYS93 |
E | ASP95 |
E | GLU96 |
site_id | AC3 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE GOL B 301 |
Chain | Residue |
A | LYS93 |
A | ASP95 |
A | GLU96 |
A | HOH428 |
B | GLN155 |
B | SER197 |
B | LEU198 |
B | LYS203 |
B | PEG302 |
B | HOH411 |
B | HOH435 |
site_id | AC4 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE PEG B 302 |
Chain | Residue |
B | ARG18 |
B | LEU20 |
B | GLN155 |
B | LEU158 |
B | LEU159 |
B | GLN162 |
B | GLY199 |
B | GOL301 |
B | HOH404 |
B | HOH411 |
B | HOH417 |
B | HOH428 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE TRS B 303 |
Chain | Residue |
B | HIS12 |
B | LEU16 |
B | LEU24 |
B | LYS26 |
B | HOH421 |
site_id | AC6 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE GTP B 304 |
Chain | Residue |
B | ARG64 |
B | THR86 |
B | VAL130 |
B | ILE131 |
B | GLY132 |
B | LEU133 |
B | SER134 |
B | LYS135 |
B | ARG138 |
C | HIS111 |
C | HIS112 |
C | VAL149 |
C | GLN150 |
C | GLU151 |
C | HIS178 |
C | CYS180 |
C | ARG184 |
C | CA304 |
site_id | AC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CA B 305 |
Chain | Residue |
A | GTP301 |
B | CYS109 |
B | HIS111 |
B | HIS112 |
B | CYS180 |
site_id | AC8 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL C 301 |
Chain | Residue |
B | ASP95 |
B | GLU96 |
C | GLN155 |
C | SER197 |
C | LEU198 |
C | LYS203 |
C | HOH443 |
site_id | AC9 |
Number of Residues | 24 |
Details | BINDING SITE FOR RESIDUE GTP C 302 |
Chain | Residue |
D | HIS111 |
D | HIS112 |
D | VAL149 |
D | GLN150 |
D | GLU151 |
D | HIS178 |
D | CYS180 |
D | ARG184 |
D | GLY185 |
D | CA304 |
D | HOH422 |
A | ARG64 |
C | LYS84 |
C | THR86 |
C | VAL130 |
C | ILE131 |
C | GLY132 |
C | LEU133 |
C | SER134 |
C | LYS135 |
C | ARG138 |
C | HOH421 |
C | HOH436 |
D | CYS109 |
site_id | BC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE TRS C 303 |
Chain | Residue |
C | HIS12 |
C | LEU16 |
C | LEU24 |
C | LYS26 |
site_id | BC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CA C 304 |
Chain | Residue |
B | GTP304 |
C | CYS109 |
C | HIS111 |
C | HIS112 |
C | CYS180 |
site_id | BC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GOL C 305 |
Chain | Residue |
A | ARG37 |
B | HIS41 |
C | ARG37 |
D | HIS47 |
site_id | BC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GOL C 306 |
Chain | Residue |
C | ASP117 |
C | LYS119 |
C | ASP175 |
C | VAL177 |
site_id | BC5 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL D 301 |
Chain | Residue |
C | LYS93 |
C | ASP95 |
C | GLU96 |
D | GLN155 |
D | LEU158 |
D | LEU198 |
D | LYS203 |
site_id | BC6 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE GTP D 302 |
Chain | Residue |
D | THR86 |
D | VAL130 |
D | ILE131 |
D | GLY132 |
D | LEU133 |
D | SER134 |
D | LYS135 |
D | ARG138 |
E | ARG64 |
E | CYS109 |
E | HIS111 |
E | HIS112 |
E | VAL149 |
E | GLN150 |
E | GLU151 |
E | HIS178 |
E | CYS180 |
E | ARG184 |
site_id | BC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE TRS D 303 |
Chain | Residue |
D | HIS12 |
D | LEU16 |
D | LEU24 |
D | ARG25 |
D | LYS26 |
D | HOH420 |
site_id | BC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CA D 304 |
Chain | Residue |
C | GTP302 |
D | CYS109 |
D | HIS111 |
D | HIS112 |
D | CYS180 |
site_id | BC9 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL E 301 |
Chain | Residue |
D | ASP95 |
D | GLU96 |
E | GLN155 |
E | LEU158 |
E | SER197 |
E | LEU198 |
E | LYS203 |
site_id | CC1 |
Number of Residues | 20 |
Details | BINDING SITE FOR RESIDUE GTP E 302 |
Chain | Residue |
A | CYS109 |
A | HIS111 |
A | HIS112 |
A | VAL149 |
A | GLN150 |
A | GLU151 |
A | HIS178 |
A | CYS180 |
A | ARG184 |
A | HOH434 |
D | ARG64 |
E | THR86 |
E | VAL130 |
E | ILE131 |
E | GLY132 |
E | LEU133 |
E | SER134 |
E | LYS135 |
E | ARG138 |
E | HOH414 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 15 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00223 |
Chain | Residue | Details |
A | CYS109 | |
D | CYS109 | |
D | HIS112 | |
D | CYS180 | |
E | CYS109 | |
E | HIS112 | |
E | CYS180 | |
A | HIS112 | |
A | CYS180 | |
B | CYS109 | |
B | HIS112 | |
B | CYS180 | |
C | CYS109 | |
C | HIS112 | |
C | CYS180 |