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5IAV

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

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
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
B0031418molecular_functionL-ascorbic acid binding
B0046872molecular_functionmetal ion binding
B0051213molecular_functiondioxygenase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue CO A 301
ChainResidue
AHIS127
AASP129
AHIS193
AMLI302
AHOH495
AHOH506

site_idAC2
Number of Residues9
Detailsbinding site for residue MLI A 302
ChainResidue
AHIS193
AGLY195
ALYS203
AILE205
ACO301
AHOH495
ATYR124
AHIS127
ATHR159

site_idAC3
Number of Residues6
Detailsbinding site for residue CO B 301
ChainResidue
BHIS127
BASP129
BHIS193
BMLI302
BHOH476
BHOH487

site_idAC4
Number of Residues9
Detailsbinding site for residue MLI B 302
ChainResidue
BTYR124
BHIS127
BTHR159
BHIS193
BGLY195
BLYS203
BILE205
BCO301
BHOH476

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PDB entries from 2024-06-12

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