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1YI9

Crystal Structure Analysis of the oxidized form of the M314I mutant of Peptidylglycine alpha-Hydroxylating Monooxygenase

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 Residues2
DetailsBINDING SITE FOR RESIDUE CU A 357
ChainResidue
AHIS108
AHIS172

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CU A 360
ChainResidue
AGLU128
AHIS279
AHOH715
AHOH778
AHOH832
AHOH833

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CU A 361
ChainResidue
AGLU313
AHOH838
AHIS245

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CU A 358
ChainResidue
AHIS242
AHIS244
AHOH842

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 703
ChainResidue
ATYR205
AGLN228
ATYR229
ALYS230
AMET231
AMET332
AHOH789

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 710
ChainResidue
ALYS219
ATYR253
ALEU262
AARG265
APRO347
AGLU349

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
AILE314

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1opm
ChainResidueDetails
AHIS242
AGLN170
AHIS108

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
AILE314metal ligand

237992

PDB entries from 2025-06-25

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