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5O1M

Structure of Latex Clearing Protein LCP in the closed state

Functional Information from GO Data
ChainGOidnamespacecontents
A0005576cellular_componentextracellular region
A0008300biological_processisoprenoid catabolic process
A0016491molecular_functionoxidoreductase activity
A0016701molecular_functionoxidoreductase activity, acting on single donors with incorporation of molecular oxygen
A0020037molecular_functionheme binding
A0046872molecular_functionmetal ion binding
B0005576cellular_componentextracellular region
B0008300biological_processisoprenoid catabolic process
B0016491molecular_functionoxidoreductase activity
B0016701molecular_functionoxidoreductase activity, acting on single donors with incorporation of molecular oxygen
B0020037molecular_functionheme binding
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues15
Detailsbinding site for residue HEM A 600
ChainResidue
AARG147
ATHR194
AVAL197
AHIS198
AASP226
ATHR230
AHOH708
AGLU148
AALA151
ASER155
AGLY158
AALA159
AARG164
ALYS167
ALEU171

site_idAC2
Number of Residues13
Detailsbinding site for residue HEM B 501
ChainResidue
BALA151
BSER155
BGLY158
BALA159
BARG164
BLYS167
BLEU171
BTHR194
BVAL197
BHIS198
BVAL201
BTHR230
BHOH627

site_idAC3
Number of Residues8
Detailsbinding site for residue EDO B 502
ChainResidue
BASP56
BARG195
BHIS198
BARG202
BILE227
BLEU268
BHOH604
BHOH607

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: axial binding residue => ECO:0000305|PubMed:27590810
ChainResidueDetails
AHIS198
BHIS198

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PDB entries from 2025-06-18

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