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2I6K

Crystal structure of human type I IPP isomerase complexed with a substrate analog

Functional Information from GO Data
ChainGOidnamespacecontents
A0004452molecular_functionisopentenyl-diphosphate delta-isomerase activity
A0005737cellular_componentcytoplasm
A0005777cellular_componentperoxisome
A0005829cellular_componentcytosol
A0006629biological_processlipid metabolic process
A0006694biological_processsteroid biosynthetic process
A0006695biological_processcholesterol biosynthetic process
A0008202biological_processsteroid metabolic process
A0008203biological_processcholesterol metabolic process
A0008299biological_processisoprenoid biosynthetic process
A0009240biological_processisopentenyl diphosphate biosynthetic process
A0010142biological_processfarnesyl diphosphate biosynthetic process, mevalonate pathway
A0016126biological_processsterol biosynthetic process
A0016853molecular_functionisomerase activity
A0016860molecular_functionintramolecular oxidoreductase activity
A0033386biological_processgeranylgeranyl diphosphate biosynthetic process
A0033489biological_processcholesterol biosynthetic process via desmosterol
A0033490biological_processcholesterol biosynthetic process via lathosterol
A0035634biological_processresponse to stilbenoid
A0036197biological_processzymosterol biosynthetic process
A0046872molecular_functionmetal ion binding
A0050992biological_processdimethylallyl diphosphate biosynthetic process
B0004452molecular_functionisopentenyl-diphosphate delta-isomerase activity
B0005737cellular_componentcytoplasm
B0005777cellular_componentperoxisome
B0005829cellular_componentcytosol
B0006629biological_processlipid metabolic process
B0006694biological_processsteroid biosynthetic process
B0006695biological_processcholesterol biosynthetic process
B0008202biological_processsteroid metabolic process
B0008203biological_processcholesterol metabolic process
B0008299biological_processisoprenoid biosynthetic process
B0009240biological_processisopentenyl diphosphate biosynthetic process
B0010142biological_processfarnesyl diphosphate biosynthetic process, mevalonate pathway
B0016126biological_processsterol biosynthetic process
B0016853molecular_functionisomerase activity
B0016860molecular_functionintramolecular oxidoreductase activity
B0033386biological_processgeranylgeranyl diphosphate biosynthetic process
B0033489biological_processcholesterol biosynthetic process via desmosterol
B0033490biological_processcholesterol biosynthetic process via lathosterol
B0035634biological_processresponse to stilbenoid
B0036197biological_processzymosterol biosynthetic process
B0046872molecular_functionmetal ion binding
B0050992biological_processdimethylallyl diphosphate biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MN A 228
ChainResidue
AHIS40
AHIS51
AHIS88
AGLU146
AGLU148

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 302
ChainResidue
AHOH515
AHOH541
ACYS86
ASER87
AGLU115
AEA2401

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 303
ChainResidue
AGLU97
ASER99
AHOH521
AHOH556
AHOH557
BHOH552

site_idAC4
Number of Residues17
DetailsBINDING SITE FOR RESIDUE EA2 A 401
ChainResidue
ALYS36
AARG70
ALYS74
ACYS86
ASER87
AHIS88
AARG111
AGLU115
ATYR136
AGLU146
AGLU148
AMG302
AHOH515
AHOH541
AHOH548
AHOH549
AHOH567

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ACY A 501
ChainResidue
AASP28
AGLU98
AARG133

site_idAC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ACY A 502
ChainResidue
AGLU26
AASN27

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ACY A 503
ChainResidue
ALEU183
AALA186
AALA187
ALYS198

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MN B 228
ChainResidue
BHIS40
BHIS51
BHIS88
BGLU146
BGLU148

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG B 301
ChainResidue
BCYS86
BSER87
BGLU115
BEA2402
BHOH508
BHOH549

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG B 304
ChainResidue
BGLU97
BSER99
BHOH558
BHOH559

site_idBC2
Number of Residues16
DetailsBINDING SITE FOR RESIDUE EA2 B 402
ChainResidue
BLYS36
BARG70
BLYS74
BCYS86
BSER87
BHIS88
BARG111
BGLU115
BTYR136
BGLU146
BGLU148
BMG301
BHOH508
BHOH517
BHOH549
BHOH564

site_idBC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ACY B 504
ChainResidue
AARG110
BLYS30
BILE31
BHOH518

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsActive site: {}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"17250851","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues8
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1i9a
ChainResidueDetails
AGLU148
ACYS86
AGLU115
ATRP196

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1i9a
ChainResidueDetails
BGLU148
BCYS86
BGLU115
BTRP196

246031

PDB entries from 2025-12-10

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