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3ITQ

Crystal Structure of a Prolyl 4-Hydroxylase from Bacillus anthracis

Functional Information from GO Data
ChainGOidnamespacecontents
A0003674molecular_functionmolecular_function
A0004656molecular_functionprocollagen-proline 4-dioxygenase activity
A0005506molecular_functioniron ion binding
A0008150biological_processbiological_process
A0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
A0018401biological_processpeptidyl-proline hydroxylation to 4-hydroxy-L-proline
A0031418molecular_functionL-ascorbic acid binding
A0046872molecular_functionmetal ion binding
A0051213molecular_functiondioxygenase activity
B0003674molecular_functionmolecular_function
B0004656molecular_functionprocollagen-proline 4-dioxygenase activity
B0005506molecular_functioniron ion binding
B0008150biological_processbiological_process
B0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
B0018401biological_processpeptidyl-proline hydroxylation to 4-hydroxy-L-proline
B0031418molecular_functionL-ascorbic acid binding
B0046872molecular_functionmetal ion binding
B0051213molecular_functiondioxygenase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 968
ChainResidue
ATYR124
AHIS127
AASP129
AHIS193
ATRP209

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 A 217
ChainResidue
BHIS169
ALYS35
AGLU37
BGLU158
BSER167

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 B 218
ChainResidue
AGLU158
ASER167
AHIS169
BLYS35
BGLU37

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL B 969
ChainResidue
BTYR124
BHIS127
BASP129
BVAL147
BPHE178
BHIS193

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PDB entries from 2024-10-02

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