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2FGE

Crystal structure of presequence protease PreP from Arabidopsis thaliana

Functional Information from GO Data
ChainGOidnamespacecontents
A0004222molecular_functionmetalloendopeptidase activity
A0005515molecular_functionprotein binding
A0005739cellular_componentmitochondrion
A0005759cellular_componentmitochondrial matrix
A0005829cellular_componentcytosol
A0006508biological_processproteolysis
A0008237molecular_functionmetallopeptidase activity
A0009507cellular_componentchloroplast
A0009570cellular_componentchloroplast stroma
A0009941cellular_componentchloroplast envelope
A0016485biological_processprotein processing
A0046872molecular_functionmetal ion binding
A0048046cellular_componentapoplast
B0004222molecular_functionmetalloendopeptidase activity
B0005515molecular_functionprotein binding
B0005739cellular_componentmitochondrion
B0005759cellular_componentmitochondrial matrix
B0005829cellular_componentcytosol
B0006508biological_processproteolysis
B0008237molecular_functionmetallopeptidase activity
B0009507cellular_componentchloroplast
B0009570cellular_componentchloroplast stroma
B0009941cellular_componentchloroplast envelope
B0016485biological_processprotein processing
B0046872molecular_functionmetal ion binding
B0048046cellular_componentapoplast
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 996
ChainResidue
AHIS77
AHIS81
AGLU177
DTHR4

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 996
ChainResidue
BHIS77
BHIS81
BGLU177
ETHR4

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 997
ChainResidue
ATHR202
ALYS271
AHOH1389
AASN201

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL B 997
ChainResidue
BASN201
BTHR202
BLYS271

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 998
ChainResidue
AASP705
AHOH1000
AHOH1001
AHOH1002
AHOH1003
AHOH1004

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MG A 999
ChainResidue
AASP510
AHOH1005
AHOH1006
AHOH1007
AHOH1008
AHOH1009
AHOH1010

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG B 998
ChainResidue
BASP705
BHOH1000
BHOH1001
BHOH1002
BHOH1003
BHOH1004

site_idAC8
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MG B 999
ChainResidue
BASP952
BHOH1005
BHOH1006
BHOH1007
BHOH1008
BHOH1009
BHOH1010

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000269|PubMed:16601675
ChainResidueDetails
ALEU108
BLEU108

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000305|PubMed:14617063, ECO:0000305|PubMed:16601675, ECO:0007744|PDB:2FGE
ChainResidueDetails
ASER183
BSER183

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:16601675
ChainResidueDetails
AHIS105
AASN109
AVAL205
BHIS105
BASN109
BVAL205

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:16601675, ECO:0007744|PDB:2FGE
ChainResidueDetails
AGLY648
BGLY648

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: N-acetylvaline => ECO:0007744|PubMed:22223895
ChainResidueDetails
APHE29
BPHE29

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1hr6
ChainResidueDetails
AGLN80

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1hr6
ChainResidueDetails
BGLN80

222415

PDB entries from 2024-07-10

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