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1YEW

Crystal structure of particulate methane monooxygenase

Functional Information from GO Data
ChainGOidnamespacecontents
A0004497molecular_functionmonooxygenase activity
A0016020cellular_componentmembrane
A0016491molecular_functionoxidoreductase activity
A0046872molecular_functionmetal ion binding
B0004497molecular_functionmonooxygenase activity
B0016020cellular_componentmembrane
B0016491molecular_functionoxidoreductase activity
C0004497molecular_functionmonooxygenase activity
C0046872molecular_functionmetal ion binding
E0004497molecular_functionmonooxygenase activity
E0016020cellular_componentmembrane
E0016491molecular_functionoxidoreductase activity
E0046872molecular_functionmetal ion binding
F0004497molecular_functionmonooxygenase activity
F0016020cellular_componentmembrane
F0016491molecular_functionoxidoreductase activity
G0004497molecular_functionmonooxygenase activity
G0046872molecular_functionmetal ion binding
I0004497molecular_functionmonooxygenase activity
I0016020cellular_componentmembrane
I0016491molecular_functionoxidoreductase activity
I0046872molecular_functionmetal ion binding
J0004497molecular_functionmonooxygenase activity
J0016020cellular_componentmembrane
J0016491molecular_functionoxidoreductase activity
K0004497molecular_functionmonooxygenase activity
K0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN C 661
ChainResidue
BGLU195
CASP156
CHIS160
CHIS173

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CU A 4
ChainResidue
AHIS48
AHIS72
AGLN404

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN G 662
ChainResidue
GHIS160
GHIS173
FGLU195
GASP156

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CU E 501
ChainResidue
EHIS48
EHIS72
EGLN404

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN K 663
ChainResidue
JGLU195
KASP156
KHIS160
KHIS173

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CU I 601
ChainResidue
IHIS48
IHIS72
IGLN404

site_idAC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ZN A 800
ChainResidue
AGLU57
EASP328

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN E 900
ChainResidue
EASP326
EASP328
EASP344
EZN702

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN C 700
ChainResidue
BHIS11
BHIS11
CHIS231
CHIS231

site_idBC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ZN E 701
ChainResidue
ETHR305
EHIS307
EHIS307

site_idBC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ZN E 702
ChainResidue
ESER347
EZN900

site_idBC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CUA A 3
ChainResidue
AHIS33
AHIS137
AHIS139
AGLY154

site_idBC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CUA E 500
ChainResidue
EHIS33
EHIS137
EHIS139
EGLY154

site_idBC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CUA I 600
ChainResidue
IHIS33
IHIS137
IHIS139
IGLY154

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues480
DetailsTransmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues864
DetailsRegion: {"description":"Cupredoxin domain used to construct soluble pmoB (spmoB)"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues15
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"15674245","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22013879","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1YEW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3RGB","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

246905

PDB entries from 2025-12-31

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