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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

3MIH

Oxidized (Cu2+) peptidylglycine alpha-hydroxylating monooxygenase (PHM) with bound azide, obtained in the presence of substrate

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
AAZI3
AHIS242
AHIS244
AMET314
site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NI A 359
ChainResidue
AHIS305
AHOH367
AHOH368
AHOH370
AAZI4
AHIS235
site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE IOD A 360
ChainResidue
ASER190
AHIS192
site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE NA A 363
ChainResidue
AAZI1
AASP96
AHIS192
site_idAC6
Number of Residues1
DetailsBINDING SITE FOR RESIDUE NA A 364
ChainResidue
AAZI5
site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE NA A 365
ChainResidue
AAZI7
AGLY299
AARG300
site_idAC8
Number of Residues2
DetailsBINDING SITE FOR RESIDUE NA A 366
ChainResidue
AAZI3
ACYS126
site_idAC9
Number of Residues2
DetailsBINDING SITE FOR RESIDUE AZI A 1
ChainResidue
AHIS192
ANA363
site_idBC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE AZI A 3
ChainResidue
AHIS242
AHIS244
AGLY308
ACU358
ANA366
site_idBC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE AZI A 4
ChainResidue
AHIS235
AALA303
ATHR304
AHIS305
AASP312
ANI359
AHOH370
site_idBC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE AZI A 5
ChainResidue
ANA364
site_idBC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE AZI A 7
ChainResidue
AHIS245
ANA365
site_idBC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE AZI A 8
ChainResidue
AVAL255
AASN257
AGLY258
AGLY286
AILE288
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 Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"10504734","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15131304","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16100265","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20958070","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23247335","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36880254","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1OPM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1SDW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1YIP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3MIB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3PHM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4E4Z","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8DSJ","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"10504734","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15131304","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16100265","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20958070","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23247335","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30271955","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36880254","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1OPM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1SDW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1YIP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3MIB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3PHM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4E4Z","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6ALV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8DSJ","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"10504734","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15131304","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20958070","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23247335","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30271955","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36880254","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1OPM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1SDW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3MIB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3PHM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4E4Z","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6ALV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8DSJ","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
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

238895

PDB entries from 2025-07-16

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