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3AAK

Crystal structure of Zn2+-bound form of des3-20ALG-2F122A

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0001525biological_processangiogenesis
A0001938biological_processpositive regulation of endothelial cell proliferation
A0005509molecular_functioncalcium ion binding
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005768cellular_componentendosome
A0005783cellular_componentendoplasmic reticulum
A0005789cellular_componentendoplasmic reticulum membrane
A0005829cellular_componentcytosol
A0006886biological_processintracellular protein transport
A0006888biological_processendoplasmic reticulum to Golgi vesicle-mediated transport
A0006915biological_processapoptotic process
A0010595biological_processpositive regulation of endothelial cell migration
A0012507cellular_componentER to Golgi transport vesicle membrane
A0014029biological_processneural crest formation
A0014032biological_processneural crest cell development
A0030127cellular_componentCOPII vesicle coat
A0030674molecular_functionprotein-macromolecule adaptor activity
A0030948biological_processnegative regulation of vascular endothelial growth factor receptor signaling pathway
A0031410cellular_componentcytoplasmic vesicle
A0031463cellular_componentCul3-RING ubiquitin ligase complex
A0032007biological_processnegative regulation of TOR signaling
A0034605biological_processcellular response to heat
A0036324biological_processvascular endothelial growth factor receptor-2 signaling pathway
A0042802molecular_functionidentical protein binding
A0042803molecular_functionprotein homodimerization activity
A0043065biological_processpositive regulation of apoptotic process
A0043495molecular_functionprotein-membrane adaptor activity
A0045766biological_processpositive regulation of angiogenesis
A0046872molecular_functionmetal ion binding
A0046982molecular_functionprotein heterodimerization activity
A0046983molecular_functionprotein dimerization activity
A0048208biological_processCOPII vesicle coating
A0048306molecular_functioncalcium-dependent protein binding
A0048471cellular_componentperinuclear region of cytoplasm
A0051592biological_processresponse to calcium ion
A0051898biological_processnegative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction
A0070062cellular_componentextracellular exosome
A0070971cellular_componentendoplasmic reticulum exit site
A0097190biological_processapoptotic signaling pathway
A1902527biological_processpositive regulation of protein monoubiquitination
A1990756molecular_functionubiquitin-like ligase-substrate adaptor activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN A 991
ChainResidue
AHOH14
AASP36
AASP38
ASER40
AVAL42
AGLU47

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN A 992
ChainResidue
ASER107
AMET109
AGLU114
AHOH12
AASP103
AASP105

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 993
ChainResidue
AHOH15
AHOH16
AASP128
AASP171
AASP173

Functional Information from PROSITE/UniProt
site_idPS00018
Number of Residues13
DetailsEF_HAND_1 EF-hand calcium-binding domain. DKDRSGVISdtEL
ChainResidueDetails
AASP36-LEU48
AASP103-LEU115

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues30
DetailsDomain: {"description":"EF-hand 2","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues35
DetailsDomain: {"description":"EF-hand 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues35
DetailsDomain: {"description":"EF-hand 4","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues29
DetailsDomain: {"description":"EF-hand 5","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues9
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"18940611","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18997320","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20691033","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25667979","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"18940611","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18997320","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20691033","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25667979","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P12815","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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