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4F1E

The Crystal Structure of a Human MitoNEET mutant with Asp 67 replaced by a Gly

Functional Information from GO Data
ChainGOidnamespacecontents
A0010506biological_processregulation of autophagy
A0043231cellular_componentintracellular membrane-bounded organelle
A0051537molecular_function2 iron, 2 sulfur cluster binding
B0010506biological_processregulation of autophagy
B0043231cellular_componentintracellular membrane-bounded organelle
B0051537molecular_function2 iron, 2 sulfur cluster binding
C0010506biological_processregulation of autophagy
C0043231cellular_componentintracellular membrane-bounded organelle
C0051537molecular_function2 iron, 2 sulfur cluster binding
D0010506biological_processregulation of autophagy
D0043231cellular_componentintracellular membrane-bounded organelle
D0051537molecular_function2 iron, 2 sulfur cluster binding
E0010506biological_processregulation of autophagy
E0043231cellular_componentintracellular membrane-bounded organelle
E0051537molecular_function2 iron, 2 sulfur cluster binding
F0010506biological_processregulation of autophagy
F0043231cellular_componentintracellular membrane-bounded organelle
F0051537molecular_function2 iron, 2 sulfur cluster binding
G0010506biological_processregulation of autophagy
G0043231cellular_componentintracellular membrane-bounded organelle
G0051537molecular_function2 iron, 2 sulfur cluster binding
H0010506biological_processregulation of autophagy
H0043231cellular_componentintracellular membrane-bounded organelle
H0051537molecular_function2 iron, 2 sulfur cluster binding
I0010506biological_processregulation of autophagy
I0043231cellular_componentintracellular membrane-bounded organelle
I0051537molecular_function2 iron, 2 sulfur cluster binding
J0010506biological_processregulation of autophagy
J0043231cellular_componentintracellular membrane-bounded organelle
J0051537molecular_function2 iron, 2 sulfur cluster binding
K0010506biological_processregulation of autophagy
K0043231cellular_componentintracellular membrane-bounded organelle
K0051537molecular_function2 iron, 2 sulfur cluster binding
L0010506biological_processregulation of autophagy
L0043231cellular_componentintracellular membrane-bounded organelle
L0051537molecular_function2 iron, 2 sulfur cluster binding
M0010506biological_processregulation of autophagy
M0043231cellular_componentintracellular membrane-bounded organelle
M0051537molecular_function2 iron, 2 sulfur cluster binding
N0010506biological_processregulation of autophagy
N0043231cellular_componentintracellular membrane-bounded organelle
N0051537molecular_function2 iron, 2 sulfur cluster binding
O0010506biological_processregulation of autophagy
O0043231cellular_componentintracellular membrane-bounded organelle
O0051537molecular_function2 iron, 2 sulfur cluster binding
P0010506biological_processregulation of autophagy
P0043231cellular_componentintracellular membrane-bounded organelle
P0051537molecular_function2 iron, 2 sulfur cluster binding
Q0010506biological_processregulation of autophagy
Q0043231cellular_componentintracellular membrane-bounded organelle
Q0051537molecular_function2 iron, 2 sulfur cluster binding
R0010506biological_processregulation of autophagy
R0043231cellular_componentintracellular membrane-bounded organelle
R0051537molecular_function2 iron, 2 sulfur cluster binding
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE FES A 201
ChainResidue
ACYS72
AARG73
ACYS74
ACYS83
AASP84
AALA86
AHIS87
APRO100

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE FES B 201
ChainResidue
BARG73
BCYS74
BCYS83
BASP84
BALA86
BHIS87
BCYS72

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE FES C 201
ChainResidue
CCYS72
CARG73
CCYS74
CSER77
CCYS83
CASP84
CALA86
CHIS87

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE FES D 500
ChainResidue
DCYS72
DARG73
DCYS74
DSER77
DCYS83
DASP84
DALA86
DHIS87

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE FES E 201
ChainResidue
ECYS72
EARG73
ECYS74
ECYS83
EASP84
EGLY85
EALA86
EHIS87

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE FES F 201
ChainResidue
FCYS72
FARG73
FCYS74
FCYS83
FASP84
FALA86
FHIS87

site_idAC7
Number of Residues8
DetailsBINDING SITE FOR RESIDUE FES G 201
ChainResidue
GCYS72
GARG73
GCYS74
GCYS83
GASP84
GGLY85
GALA86
GHIS87

site_idAC8
Number of Residues8
DetailsBINDING SITE FOR RESIDUE FES H 201
ChainResidue
HCYS72
HARG73
HCYS74
HSER77
HCYS83
HASP84
HALA86
HHIS87

site_idAC9
Number of Residues8
DetailsBINDING SITE FOR RESIDUE FES I 201
ChainResidue
ICYS72
IARG73
ICYS74
ICYS83
IASP84
IGLY85
IALA86
IHIS87

site_idBC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE FES J 201
ChainResidue
JCYS72
JARG73
JCYS74
JCYS83
JASP84
JGLY85
JALA86
JHIS87

site_idBC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE FES K 201
ChainResidue
KCYS72
KARG73
KCYS74
KCYS83
KASP84
KGLY85
KALA86
KHIS87

site_idBC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE FES L 201
ChainResidue
LCYS72
LARG73
LCYS74
LCYS83
LASP84
LGLY85
LALA86
LHIS87

site_idBC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE FES M 201
ChainResidue
MASP84
MGLY85
MALA86
MHIS87
MCYS72
MARG73
MCYS74
MSER77
MCYS83

site_idBC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE FES N 201
ChainResidue
NCYS72
NARG73
NCYS74
NCYS83
NASP84
NALA86
NHIS87

site_idBC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE FES O 201
ChainResidue
OCYS72
OARG73
OCYS74
OCYS83
OASP84
OALA86
OHIS87

site_idBC7
Number of Residues8
DetailsBINDING SITE FOR RESIDUE FES P 201
ChainResidue
PCYS72
PARG73
PCYS74
PSER77
PCYS83
PASP84
PALA86
PHIS87

site_idBC8
Number of Residues7
DetailsBINDING SITE FOR RESIDUE FES Q 201
ChainResidue
QCYS72
QARG73
QCYS74
QCYS83
QASP84
QALA86
QHIS87

site_idBC9
Number of Residues8
DetailsBINDING SITE FOR RESIDUE FES R 201
ChainResidue
RCYS72
RARG73
RCYS74
RSER77
RCYS83
RASP84
RALA86
RHIS87

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues18
DetailsActive site: {"description":"Schiff-base intermediate with pyridoxal 5'-phosphate","evidences":[{"source":"PubMed","id":"36194135","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues72
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"17766439","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17766440","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17905743","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2QD0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2QH7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2R13","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues54
DetailsModified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q91WS0","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues118
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"25621951","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues54
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate","evidences":[{"source":"PubMed","id":"25621951","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

243083

PDB entries from 2025-10-15

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