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5H7D

Crystal structure of the YgjG-protein A-Zpa963-calmodulin complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0005829cellular_componentcytosol
A0008483molecular_functiontransaminase activity
A0009447biological_processputrescine catabolic process
A0016740molecular_functiontransferase activity
A0019161molecular_functiondiamine transaminase activity
A0019477biological_processL-lysine catabolic process
A0019865molecular_functionimmunoglobulin binding
A0030170molecular_functionpyridoxal phosphate binding
A0033094molecular_functionputrescine--2-oxoglutarate transaminase activity
A0042802molecular_functionidentical protein binding
A0042803molecular_functionprotein homodimerization activity
B0005829cellular_componentcytosol
B0008483molecular_functiontransaminase activity
B0009447biological_processputrescine catabolic process
B0016740molecular_functiontransferase activity
B0019161molecular_functiondiamine transaminase activity
B0019477biological_processL-lysine catabolic process
B0019865molecular_functionimmunoglobulin binding
B0030170molecular_functionpyridoxal phosphate binding
B0033094molecular_functionputrescine--2-oxoglutarate transaminase activity
B0042802molecular_functionidentical protein binding
B0042803molecular_functionprotein homodimerization activity
C0005829cellular_componentcytosol
C0008483molecular_functiontransaminase activity
C0009447biological_processputrescine catabolic process
C0016740molecular_functiontransferase activity
C0019161molecular_functiondiamine transaminase activity
C0019477biological_processL-lysine catabolic process
C0019865molecular_functionimmunoglobulin binding
C0030170molecular_functionpyridoxal phosphate binding
C0033094molecular_functionputrescine--2-oxoglutarate transaminase activity
C0042802molecular_functionidentical protein binding
C0042803molecular_functionprotein homodimerization activity
D0005829cellular_componentcytosol
D0008483molecular_functiontransaminase activity
D0009447biological_processputrescine catabolic process
D0016740molecular_functiontransferase activity
D0019161molecular_functiondiamine transaminase activity
D0019477biological_processL-lysine catabolic process
D0019865molecular_functionimmunoglobulin binding
D0030170molecular_functionpyridoxal phosphate binding
D0033094molecular_functionputrescine--2-oxoglutarate transaminase activity
D0042802molecular_functionidentical protein binding
D0042803molecular_functionprotein homodimerization activity
E0005509molecular_functioncalcium ion binding
E0019865molecular_functionimmunoglobulin binding
F0005509molecular_functioncalcium ion binding
F0019865molecular_functionimmunoglobulin binding
G0005509molecular_functioncalcium ion binding
G0019865molecular_functionimmunoglobulin binding
H0005509molecular_functioncalcium ion binding
H0019865molecular_functionimmunoglobulin binding
I0005829cellular_componentcytosol
I0008483molecular_functiontransaminase activity
I0009447biological_processputrescine catabolic process
I0016740molecular_functiontransferase activity
I0019161molecular_functiondiamine transaminase activity
I0019477biological_processL-lysine catabolic process
I0019865molecular_functionimmunoglobulin binding
I0030170molecular_functionpyridoxal phosphate binding
I0033094molecular_functionputrescine--2-oxoglutarate transaminase activity
I0042802molecular_functionidentical protein binding
I0042803molecular_functionprotein homodimerization activity
J0005829cellular_componentcytosol
J0008483molecular_functiontransaminase activity
J0009447biological_processputrescine catabolic process
J0016740molecular_functiontransferase activity
J0019161molecular_functiondiamine transaminase activity
J0019477biological_processL-lysine catabolic process
J0019865molecular_functionimmunoglobulin binding
J0030170molecular_functionpyridoxal phosphate binding
J0033094molecular_functionputrescine--2-oxoglutarate transaminase activity
J0042802molecular_functionidentical protein binding
J0042803molecular_functionprotein homodimerization activity
K0005509molecular_functioncalcium ion binding
K0019865molecular_functionimmunoglobulin binding
L0005509molecular_functioncalcium ion binding
L0019865molecular_functionimmunoglobulin binding
M0005829cellular_componentcytosol
M0008483molecular_functiontransaminase activity
M0009447biological_processputrescine catabolic process
M0016740molecular_functiontransferase activity
M0019161molecular_functiondiamine transaminase activity
M0019477biological_processL-lysine catabolic process
M0019865molecular_functionimmunoglobulin binding
M0030170molecular_functionpyridoxal phosphate binding
M0033094molecular_functionputrescine--2-oxoglutarate transaminase activity
M0042802molecular_functionidentical protein binding
M0042803molecular_functionprotein homodimerization activity
N0005829cellular_componentcytosol
N0008483molecular_functiontransaminase activity
N0009447biological_processputrescine catabolic process
N0016740molecular_functiontransferase activity
N0019161molecular_functiondiamine transaminase activity
N0019477biological_processL-lysine catabolic process
N0019865molecular_functionimmunoglobulin binding
N0030170molecular_functionpyridoxal phosphate binding
N0033094molecular_functionputrescine--2-oxoglutarate transaminase activity
N0042802molecular_functionidentical protein binding
N0042803molecular_functionprotein homodimerization activity
O0005509molecular_functioncalcium ion binding
O0019865molecular_functionimmunoglobulin binding
P0005509molecular_functioncalcium ion binding
P0019865molecular_functionimmunoglobulin binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue CA E 501
ChainResidue
EASP165
EASP167
EASP169
ETHR171
EGLU176

site_idAC2
Number of Residues5
Detailsbinding site for residue CA E 502
ChainResidue
EGLU212
EASP201
EASP203
EASN205
ETHR207

site_idAC3
Number of Residues5
Detailsbinding site for residue CA F 501
ChainResidue
FASP165
FASP167
FASP169
FTHR171
FGLU176

site_idAC4
Number of Residues5
Detailsbinding site for residue CA F 502
ChainResidue
FASP201
FASP203
FASN205
FTHR207
FGLU212

site_idAC5
Number of Residues5
Detailsbinding site for residue CA G 501
ChainResidue
GASP165
GASP167
GASP169
GTHR171
GGLU176

site_idAC6
Number of Residues5
Detailsbinding site for residue CA G 502
ChainResidue
GASP201
GASP203
GASN205
GTHR207
GGLU212

site_idAC7
Number of Residues5
Detailsbinding site for residue CA H 501
ChainResidue
HASP165
HASP167
HASP169
HTHR171
HGLU176

site_idAC8
Number of Residues5
Detailsbinding site for residue CA H 502
ChainResidue
HASP201
HASP203
HASN205
HTHR207
HGLU212

site_idAC9
Number of Residues5
Detailsbinding site for residue CA K 501
ChainResidue
KASP165
KASP167
KASP169
KTHR171
KGLU176

site_idAD1
Number of Residues5
Detailsbinding site for residue CA K 502
ChainResidue
KASP201
KASP203
KASN205
KTHR207
KGLU212

site_idAD2
Number of Residues5
Detailsbinding site for residue CA L 501
ChainResidue
LASP165
LASP167
LASP169
LTHR171
LGLU176

site_idAD3
Number of Residues5
Detailsbinding site for residue CA L 502
ChainResidue
LASP201
LASP203
LASN205
LTHR207
LGLU212

site_idAD4
Number of Residues5
Detailsbinding site for residue CA O 501
ChainResidue
OASP165
OASP167
OASP169
OTHR171
OGLU176

site_idAD5
Number of Residues5
Detailsbinding site for residue CA O 502
ChainResidue
OASP201
OASP203
OASN205
OTHR207
OGLU212

site_idAD6
Number of Residues5
Detailsbinding site for residue CA P 501
ChainResidue
PASP165
PASP167
PASP169
PTHR171
PGLU176

site_idAD7
Number of Residues5
Detailsbinding site for residue CA P 502
ChainResidue
PASP201
PASP203
PASN205
PTHR207
PGLU212

Functional Information from PROSITE/UniProt
site_idPS00018
Number of Residues13
DetailsEF_HAND_1 EF-hand calcium-binding domain. DKDGDGTITtkEL
ChainResidueDetails
EASP165-LEU177
EASP201-PHE213

site_idPS00600
Number of Residues38
DetailsAA_TRANSFER_CLASS_3 Aminotransferases class-III pyridoxal-phosphate attachment site. MIlDEVqt.GMgRtGkmfacehenvqp....DILclAKalgGG
ChainResidueDetails
AMET268-GLY305

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues16
DetailsBinding site: {"description":"in other chain","evidences":[{"source":"PubMed","id":"25423189","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"25423189","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues8
DetailsModified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"PubMed","id":"25423189","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4UOY","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues280
DetailsDomain: {"description":"EF-hand 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues80
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues8
DetailsModified residue: {"description":"N-acetylalanine","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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