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3KDS

apo-FtsH crystal structure

Functional Information from GO Data
ChainGOidnamespacecontents
E0004176molecular_functionATP-dependent peptidase activity
E0004222molecular_functionmetalloendopeptidase activity
E0005524molecular_functionATP binding
E0006508biological_processproteolysis
E0016020cellular_componentmembrane
E0016887molecular_functionATP hydrolysis activity
F0004176molecular_functionATP-dependent peptidase activity
F0004222molecular_functionmetalloendopeptidase activity
F0005524molecular_functionATP binding
F0006508biological_processproteolysis
F0016020cellular_componentmembrane
F0016887molecular_functionATP hydrolysis activity
G0004176molecular_functionATP-dependent peptidase activity
G0004222molecular_functionmetalloendopeptidase activity
G0005524molecular_functionATP binding
G0006508biological_processproteolysis
G0016020cellular_componentmembrane
G0016887molecular_functionATP hydrolysis activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN E 996
ChainResidue
EHIS423
EHIS427
EASP500
ENHX998

site_idAC2
Number of Residues13
DetailsBINDING SITE FOR RESIDUE NHX E 998
ChainResidue
EGLY454
ETYR465
ELEU466
ESER495
EGLY496
EALA498
EASP500
EZN996
EHIS423
EGLU424
EHIS427
ELYS451
ELEU453

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN F 996
ChainResidue
FHIS423
FHIS427
FASP500
FNHX998

site_idAC4
Number of Residues12
DetailsBINDING SITE FOR RESIDUE NHX F 998
ChainResidue
FHIS423
FGLU424
FHIS427
FLYS451
FALA452
FLEU453
FSER495
FGLY496
FALA498
FASP500
FZN996
GTYR465

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN G 996
ChainResidue
GHIS423
GHIS427
GASP500
GNHX998

site_idAC6
Number of Residues14
DetailsBINDING SITE FOR RESIDUE NHX G 998
ChainResidue
FTYR465
GILE420
GHIS423
GGLU424
GHIS427
GTYR450
GLYS451
GALA452
GLEU453
GGLY454
GGLY496
GASN499
GASP500
GZN996

Functional Information from PROSITE/UniProt
site_idPS00674
Number of Residues19
DetailsAAA AAA-protein family signature. IiVMaATNrpdiLDpALl.R
ChainResidueDetails
EILE300-ARG318

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: ACT_SITE => ECO:0000255|HAMAP-Rule:MF_01458, ECO:0000269|PubMed:16484367
ChainResidueDetails
EGLU424
FGLU424
GGLU424

site_idSWS_FT_FI2
Number of Residues24
DetailsBINDING: BINDING => ECO:0000269|PubMed:16484367
ChainResidueDetails
EGLY164
FGLY204
FLEU209
FHIS343
FGLU371
FHIS423
FHIS427
FASP500
GGLY164
GGLY204
GLEU209
EGLY204
GHIS343
GGLU371
GHIS423
GHIS427
GASP500
ELEU209
EHIS343
EGLU371
EHIS423
EHIS427
EASP500
FGLY164

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PDB entries from 2024-07-10

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