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5IAT

Mechanistic and Structural Analysis of Substrate Recognition and Cofactor Binding by an Unusual Bacterial Prolyl Hydroxylase - apo-BaP4H

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 Residues8
Detailsbinding site for residue GOL A 301
ChainResidue
ATYR130
AASN141
AARG142
ATYR180
APHE181
AASN188
AHOH432
BLYS68

site_idAC2
Number of Residues9
Detailsbinding site for residue GOL B 301
ChainResidue
BTYR130
BASN141
BARG142
BTYR180
BPHE181
BGLN185
BASN188
BHOH423
ALYS68

site_idAC3
Number of Residues4
Detailsbinding site for residue PEG B 302
ChainResidue
AGLU37
BPHE160
BASN165
BSER167

site_idAC4
Number of Residues5
Detailsbinding site for residue PEG B 303
ChainResidue
BLYS97
BSER100
BSER101
BVAL105
BHOH498

226707

PDB entries from 2024-10-30

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