Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

3RGB

Crystal structure of particulate methane monooxygenase from Methylococcus capsulatus (Bath)

Functional Information from GO Data
ChainGOidnamespacecontents
B0004497molecular_functionmonooxygenase activity
B0016020cellular_componentmembrane
B0016491molecular_functionoxidoreductase activity
C0004497molecular_functionmonooxygenase activity
C0015049molecular_functionmethane monooxygenase [NAD(P)H] activity
C0016491molecular_functionoxidoreductase activity
C0046872molecular_functionmetal ion binding
F0004497molecular_functionmonooxygenase activity
F0016020cellular_componentmembrane
F0016491molecular_functionoxidoreductase activity
G0004497molecular_functionmonooxygenase activity
G0015049molecular_functionmethane monooxygenase [NAD(P)H] activity
G0016491molecular_functionoxidoreductase activity
G0046872molecular_functionmetal ion binding
J0004497molecular_functionmonooxygenase activity
J0016020cellular_componentmembrane
J0016491molecular_functionoxidoreductase activity
K0004497molecular_functionmonooxygenase activity
K0015049molecular_functionmethane monooxygenase [NAD(P)H] activity
K0016491molecular_functionoxidoreductase activity
K0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CU A 415
ChainResidue
AHIS48
AHIS72
AGLN404

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ZN A 800
ChainResidue
AGLU57
EASP328

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CUA A 416
ChainResidue
AHIS33
AHIS137
AHIS139

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN C 663
ChainResidue
CHIS160
CHIS173
CHOH290
CASP156

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN B 664
ChainResidue
BHIS11
BHIS11
CALA281
CGLU284
CGLU284

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CU E 415
ChainResidue
EHIS48
EHIS72
EGLN404

site_idAC7
Number of Residues1
DetailsBINDING SITE FOR RESIDUE ZN E 800
ChainResidue
EGLY335

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CUA E 416
ChainResidue
EHIS33
EHIS137
EHIS139
EGLY154

site_idAC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CU I 415
ChainResidue
IHIS48
IHIS72
IGLN404

site_idBC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CUA I 416
ChainResidue
IHIS33
IHIS137
IHIS139

site_idBC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN K 663
ChainResidue
KASP156
KHIS160
KHIS173
KHOH290

site_idBC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE ZN J 664
ChainResidue
JHIS11

site_idBC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN G 663
ChainResidue
GASP156
GHIS160
GHIS173
GHOH290

site_idBC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ZN F 664
ChainResidue
FHIS11
GGLU284

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

249524

PDB entries from 2026-02-18

PDB statisticsPDBj update infoContact PDBjnumon