4IW3
Crystal structure of a Pseudomonas putida prolyl-4-hydroxylase (P4H) in complex with elongation factor Tu (EF-Tu)
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005506 | molecular_function | iron ion binding |
A | 0008198 | molecular_function | ferrous iron binding |
A | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
A | 0031418 | molecular_function | L-ascorbic acid binding |
A | 0031543 | molecular_function | peptidyl-proline dioxygenase activity |
A | 0046872 | molecular_function | metal ion binding |
A | 0051213 | molecular_function | dioxygenase activity |
A | 0071456 | biological_process | cellular response to hypoxia |
B | 0003746 | molecular_function | translation elongation factor activity |
B | 0003924 | molecular_function | GTPase activity |
B | 0005525 | molecular_function | GTP binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0006412 | biological_process | translation |
B | 0006414 | biological_process | translational elongation |
B | 0097216 | molecular_function | guanosine tetraphosphate binding |
J | 0005506 | molecular_function | iron ion binding |
J | 0008198 | molecular_function | ferrous iron binding |
J | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
J | 0031418 | molecular_function | L-ascorbic acid binding |
J | 0031543 | molecular_function | peptidyl-proline dioxygenase activity |
J | 0046872 | molecular_function | metal ion binding |
J | 0051213 | molecular_function | dioxygenase activity |
J | 0071456 | biological_process | cellular response to hypoxia |
K | 0003746 | molecular_function | translation elongation factor activity |
K | 0003924 | molecular_function | GTPase activity |
K | 0005525 | molecular_function | GTP binding |
K | 0005737 | cellular_component | cytoplasm |
K | 0005829 | cellular_component | cytosol |
K | 0006412 | biological_process | translation |
K | 0006414 | biological_process | translational elongation |
K | 0097216 | molecular_function | guanosine tetraphosphate binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MN A 401 |
Chain | Residue |
A | HIS124 |
A | ASP126 |
A | HIS183 |
A | OGA402 |
A | HOH563 |
site_id | AC2 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE OGA A 402 |
Chain | Residue |
A | HIS183 |
A | VAL185 |
A | ARG192 |
A | THR196 |
A | TRP198 |
A | MN401 |
A | HOH504 |
A | HOH540 |
A | HOH563 |
B | PRO54 |
A | HIS124 |
A | ASP126 |
A | TYR141 |
A | LEU154 |
site_id | AC3 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE GDP B 501 |
Chain | Residue |
B | HIS20 |
B | ASP22 |
B | HIS23 |
B | GLY24 |
B | LYS25 |
B | THR26 |
B | THR27 |
B | ASN136 |
B | LYS137 |
B | ASP139 |
B | SER174 |
B | ALA175 |
B | ARG176 |
B | ARG176 |
B | MG502 |
B | HOH616 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG B 502 |
Chain | Residue |
B | LYS25 |
B | THR26 |
B | CYS82 |
B | GDP501 |
B | HOH616 |
site_id | AC5 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE MG K 401 |
Chain | Residue |
K | THR26 |
K | ASP81 |
K | CYS82 |
K | GDP402 |
K | HOH525 |
K | HOH536 |
K | HOH537 |
site_id | AC6 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE GDP K 402 |
Chain | Residue |
K | HIS20 |
K | VAL21 |
K | ASP22 |
K | HIS23 |
K | GLY24 |
K | LYS25 |
K | THR26 |
K | THR27 |
K | ASN136 |
K | LYS137 |
K | ASP139 |
K | LEU140 |
K | SER174 |
K | ALA175 |
K | ARG176 |
K | ARG176 |
K | MG401 |
K | HOH525 |
K | HOH537 |
site_id | AC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MN J 401 |
Chain | Residue |
J | HIS124 |
J | ASP126 |
J | HIS183 |
J | OGA402 |
J | HOH532 |
site_id | AC8 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE OGA J 402 |
Chain | Residue |
J | TYR121 |
J | HIS124 |
J | ASP126 |
J | VAL139 |
J | TYR141 |
J | LEU154 |
J | HIS183 |
J | VAL185 |
J | ARG192 |
J | THR196 |
J | TRP198 |
J | MN401 |
J | HOH524 |
J | HOH532 |
J | HOH533 |
K | PRO54 |
Functional Information from PROSITE/UniProt
site_id | PS00301 |
Number of Residues | 16 |
Details | G_TR_1 Translational (tr)-type guanine nucleotide-binding (G) domain signature. DSapeEKaRGITIntA |
Chain | Residue | Details |
B | ASP51-ALA66 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00118 |
Chain | Residue | Details |
B | GLY19 | |
B | ASP81 | |
B | ASN136 | |
K | GLY19 | |
K | ASP81 | |
K | ASN136 |