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1SDW

Reduced (Cu+) peptidylglycine alpha-hydroxylating monooxygenase with bound peptide and dioxygen

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
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CU A 357
ChainResidue
AHIS107
AHIS108
AHIS172

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU A 358
ChainResidue
AHIS242
AHIS244
AMET314
AOXY360

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NI A 359
ChainResidue
AHOH361
AHOH362
AGOL363
AHIS235
AHIS305

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE OXY A 360
ChainResidue
AHIS242
AHIS244
AMET314
ACU358

site_idAC5
Number of Residues12
DetailsBINDING SITE FOR RESIDUE IYT A 701
ChainResidue
AALA135
AMET208
AARG240
AHIS242
AMET314
AASN316
ATYR318
AGOL368
AHOH406
AHOH479
AHOH491
AHOH540

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE IYT A 702
ChainResidue
AASP61
AALA63
ALYS98
AARG100
ASER190
AHIS192

site_idAC7
Number of Residues12
DetailsBINDING SITE FOR RESIDUE IYT A 703
ChainResidue
AALA59
ASER60
AASP61
APHE62
AGLU90
AGLU91
AARG195
AGLN228
ALYS230
APHE285
AGLY286
AHOH486

site_idAC8
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 363
ChainResidue
AHIS235
AHIS305
AASP312
ANI359
AHOH361
AHOH362
AHOH427
AHOH564

site_idAC9
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 364
ChainResidue
ALEU138
ATYR139
ATHR148
AMET320
AHOH401
AHOH415
AHOH423
AHOH430

site_idBC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 365
ChainResidue
AASN136
ALEU138
APHE156
AARG157
AGLY163
ASER164
ASER330
AHOH403
AHOH411

site_idBC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 366
ChainResidue
ATYR205
ACYS227
AGLN228
ALYS230
AMET231
ATHR333
AHOH487

site_idBC3
Number of Residues11
DetailsBINDING SITE FOR RESIDUE GOL A 367
ChainResidue
ATHR148
APRO151
AASP211
AVAL213
APHE237
APRO276
AHOH452
AHOH468
AHOH488
AHOH537
AHOH551

site_idBC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 368
ChainResidue
AASN136
AILE137
AMET204
ATYR318
APHE331
AMET332
ATHR333
AHOH422
AIYT701

Functional Information from PROSITE/UniProt
site_idPS00084
Number of Residues8
DetailsCU2_MONOOXYGENASE_1 Copper type II, ascorbate-dependent monooxygenases signature 1. HHMllFgC
ChainResidueDetails
AHIS107-CYS114

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 Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:10504734, ECO:0007744|PDB:1OPM, ECO:0007744|PDB:3PHM
ChainResidueDetails
AHIS107
AHIS108
AHIS172
AHIS242
AHIS244
AMET314

Catalytic Information from CSA
site_idMCSA1
Number of Residues7
DetailsM-CSA 135
ChainResidueDetails
AHIS107metal 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

218853

PDB entries from 2024-04-24

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