Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

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
DetailsActive site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01458","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16484367","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues33
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"16484367","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

PDB statisticsPDBj update infoContact PDBjnumon