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5WJA

Crystal structure of H107A peptidylglycine alpha-hydroxylating monooxygenase (PHM) in complex with citrate

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004497molecular_functionmonooxygenase activity
A0005507molecular_functioncopper ion binding
A0006518biological_processpeptide metabolic process
A0016020cellular_componentmembrane
A0016715molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced ascorbate as one donor, and incorporation of one atom of oxygen
D0003824molecular_functioncatalytic activity
D0004497molecular_functionmonooxygenase activity
D0005507molecular_functioncopper ion binding
D0006518biological_processpeptide metabolic process
D0016020cellular_componentmembrane
D0016715molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced ascorbate as one donor, and incorporation of one atom of oxygen
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue CU A 1001
ChainResidue
AHIS108
AHIS172
AHOH1140
AHOH1178

site_idAC2
Number of Residues4
Detailsbinding site for residue CU A 1002
ChainResidue
AGLU128
AHIS242
AHIS244
AMET314

site_idAC3
Number of Residues4
Detailsbinding site for residue GOL A 1003
ChainResidue
APRO87
AGLN259
ATRP260
AARG85

site_idAC4
Number of Residues4
Detailsbinding site for residue GOL A 1004
ChainResidue
ALEU262
AVAL277
AGLU278
AHIS279

site_idAC5
Number of Residues5
Detailsbinding site for residue GOL A 1005
ChainResidue
ASER209
AVAL210
AASP211
AASP224
ATHR335

site_idAC6
Number of Residues5
Detailsbinding site for residue GOL A 1006
ChainResidue
AASN136
APHE156
AARG157
ASER164
AHOH1109

site_idAC7
Number of Residues5
Detailsbinding site for residue GOL A 1007
ChainResidue
ATYR139
AALA140
ATHR148
AMET320
AHOH1129

site_idAC8
Number of Residues7
Detailsbinding site for residue GOL A 1008
ChainResidue
ASER83
AMET84
AARG85
ASER118
ASER119
ATHR120
AHOH1114

site_idAC9
Number of Residues3
Detailsbinding site for residue NI A 1009
ChainResidue
AHIS279
DHIS235
DASP282

site_idAD1
Number of Residues5
Detailsbinding site for residue CU D 1001
ChainResidue
DHIS242
DHIS244
DMET314
DFLC1002
DHOH1113

site_idAD2
Number of Residues12
Detailsbinding site for residue FLC D 1002
ChainResidue
DTYR79
DHIS108
DLEU110
DGLN170
DHIS172
DARG240
DHIS242
DASN316
DTYR318
DCU1001
DHOH1113
DHOH1127

Functional Information from PROSITE/UniProt
site_idPS00085
Number of Residues13
DetailsCU2_MONOOXYGENASE_2 Copper type II, ascorbate-dependent monooxygenases signature 2. HvFayrvHTHhlG
ChainResidueDetails
AHIS235-GLY247

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:10504734, ECO:0007744|PDB:1OPM, ECO:0007744|PDB:3PHM
ChainResidueDetails
AALA107
DHIS242
DHIS244
DMET314
AHIS108
AHIS172
AHIS242
AHIS244
AMET314
DALA107
DHIS108
DHIS172

Catalytic Information from CSA
site_idMCSA1
Number of Residues7
DetailsM-CSA 135
ChainResidueDetails
AALA107metal ligand
AHIS108hydrogen bond donor, metal ligand, single electron acceptor, single electron donor, single electron relay
AGLN170hydrogen bond acceptor, single electron acceptor, single electron donor, single electron relay
AHIS172metal ligand
AHIS242metal ligand
AHIS244metal ligand
AMET314metal ligand

site_idMCSA2
Number of Residues7
DetailsM-CSA 135
ChainResidueDetails
DALA107metal ligand
DHIS108hydrogen bond donor, metal ligand, single electron acceptor, single electron donor, single electron relay
DGLN170hydrogen bond acceptor, single electron acceptor, single electron donor, single electron relay
DHIS172metal ligand
DHIS242metal ligand
DHIS244metal ligand
DMET314metal ligand

226707

PDB entries from 2024-10-30

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