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3MIF

Oxidized (Cu2+) peptidylglycine alpha-hydroxylating monooxygenase (PHM) with bound carbon monooxide (CO)

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 Residues5
DetailsBINDING SITE FOR RESIDUE CU A 358
ChainResidue
ACMO1
AGLU128
AHIS242
AHIS244
AMET314

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NI A 359
ChainResidue
AHIS305
AHOH474
AHOH475
AHOH476
AHOH477
AHIS235

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CMO A 1
ChainResidue
AGLU128
AHIS242
AHIS244
AMET314
ACU358

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 360
ChainResidue
AHOH31
AHOH38
AHOH41
ALEU138
ATYR139
ATHR148
AMET320
AHOH369

site_idAC6
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 2
ChainResidue
AHOH11
AASN136
APHE156
AARG157
AGLY163
ASER164
ASER330
AHOH361

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 3
ChainResidue
ATYR205
AGLN228
ALYS230
AMET231
ATHR333
AHOH441

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 4
ChainResidue
AHOH29
AASP61
ATHR194
AVAL196
AGLN198

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

224572

PDB entries from 2024-09-04

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