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5HV4

Crystal Structure of a Prolyl 4-Hydroxylase Complexed with Alpha-ketoglutarate from the Pathogenic Bacterium Bacillus anthracis in C2221

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
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue CD A 301
ChainResidue
AHIS127
AASP129
AHIS193
AAKG306

site_idAC2
Number of Residues4
Detailsbinding site for residue CD A 302
ChainResidue
AASP17
AASN104
AHOH401
AHOH414

site_idAC3
Number of Residues3
Detailsbinding site for residue CD A 303
ChainResidue
AHOH461
AHOH499
AHIS18

site_idAC4
Number of Residues2
Detailsbinding site for residue CD A 304
ChainResidue
AHIS109
AASP121

site_idAC5
Number of Residues2
Detailsbinding site for residue CD A 305
ChainResidue
AGLU55
AGLU55

site_idAC6
Number of Residues7
Detailsbinding site for residue AKG A 306
ChainResidue
ATHR159
AGLY195
ALYS203
AILE205
ATHR207
ATRP209
ACD301

site_idAC7
Number of Residues2
Detailsbinding site for residue K A 307
ChainResidue
AASP54
ALYS172

site_idAC8
Number of Residues2
Detailsbinding site for residue K A 308
ChainResidue
AASP184
ASER186

site_idAC9
Number of Residues1
Detailsbinding site for residue K A 309
ChainResidue
AHIS114

site_idAD1
Number of Residues3
Detailsbinding site for residue K A 310
ChainResidue
AGLU119
AGLU202
AHOH417

site_idAD2
Number of Residues3
Detailsbinding site for residue K A 311
ChainResidue
AGLU26
AGLU154
AHOH410

site_idAD3
Number of Residues1
Detailsbinding site for residue K A 312
ChainResidue
AHIS134

226707

PDB entries from 2024-10-30

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