Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

6C56

Crystal structure of mutant human geranylgeranyl pyrophosphate synthase (Y246D) in its Apo form

Functional Information from GO Data
ChainGOidnamespacecontents
A0004161molecular_functiondimethylallyltranstransferase activity
A0004311molecular_functionfarnesyltranstransferase activity
A0004337molecular_functiongeranyltranstransferase activity
A0004659molecular_functionprenyltransferase activity
A0005515molecular_functionprotein binding
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006720biological_processisoprenoid metabolic process
A0008299biological_processisoprenoid biosynthetic process
A0016740molecular_functiontransferase activity
A0030018cellular_componentZ disc
A0033384biological_processgeranyl diphosphate biosynthetic process
A0033386biological_processgeranylgeranyl diphosphate biosynthetic process
A0042802molecular_functionidentical protein binding
A0045337biological_processfarnesyl diphosphate biosynthetic process
A0046872molecular_functionmetal ion binding
A0048471cellular_componentperinuclear region of cytoplasm
B0004161molecular_functiondimethylallyltranstransferase activity
B0004311molecular_functionfarnesyltranstransferase activity
B0004337molecular_functiongeranyltranstransferase activity
B0004659molecular_functionprenyltransferase activity
B0005515molecular_functionprotein binding
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006720biological_processisoprenoid metabolic process
B0008299biological_processisoprenoid biosynthetic process
B0016740molecular_functiontransferase activity
B0030018cellular_componentZ disc
B0033384biological_processgeranyl diphosphate biosynthetic process
B0033386biological_processgeranylgeranyl diphosphate biosynthetic process
B0042802molecular_functionidentical protein binding
B0045337biological_processfarnesyl diphosphate biosynthetic process
B0046872molecular_functionmetal ion binding
B0048471cellular_componentperinuclear region of cytoplasm
Functional Information from PDB Data
site_idAC1
Number of Residues15
Detailsbinding site for residue VT0 B 401
ChainResidue
BPRO42
BPHE166
BSER167
BLYS170
BLYS170
BHOH501
BHOH501
BASP107
BASP107
BHIS108
BHIS108
BPRO109
BLEU165
BLEU165
BPHE166

Functional Information from PROSITE/UniProt
site_idPS00444
Number of Residues13
DetailsPOLYPRENYL_SYNTHASE_2 Polyprenyl synthases signature 2. LGlfFQIrDDYaN
ChainResidueDetails
ALEU180-ASN192

site_idPS00723
Number of Residues15
DetailsPOLYPRENYL_SYNTHASE_1 Polyprenyl synthases signature 1. LLiDDie..DnsklRRG
ChainResidueDetails
ALEU61-GLY75

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P14324
ChainResidueDetails
ALYS25
AARG28
AARG74
BLYS25
BARG28
BARG74

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q12051
ChainResidueDetails
AHIS57
BHIS57

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:16698791
ChainResidueDetails
AASP64
AASP68
BASP64
BASP68

site_idSWS_FT_FI4
Number of Residues10
DetailsBINDING:
ChainResidueDetails
AARG73
BLYS202
ALYS151
ATHR152
AGLN185
ALYS202
BARG73
BLYS151
BTHR152
BGLN185

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
ALYS212
BLYS212

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: N-acetylmethionine => ECO:0007744|PubMed:22814378
ChainResidueDetails
AMET1
BMET1

222624

PDB entries from 2024-07-17

PDB statisticsPDBj update infoContact PDBjnumon