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4C3K

Structure of mixed PII-ADP complexes from S. elongatus

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005829cellular_componentcytosol
A0006808biological_processregulation of nitrogen utilization
A0030234molecular_functionenzyme regulator activity
A0042802molecular_functionidentical protein binding
B0000166molecular_functionnucleotide binding
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005829cellular_componentcytosol
B0006808biological_processregulation of nitrogen utilization
B0030234molecular_functionenzyme regulator activity
B0042802molecular_functionidentical protein binding
C0000166molecular_functionnucleotide binding
C0005515molecular_functionprotein binding
C0005524molecular_functionATP binding
C0005829cellular_componentcytosol
C0006808biological_processregulation of nitrogen utilization
C0030234molecular_functionenzyme regulator activity
C0042802molecular_functionidentical protein binding
D0000166molecular_functionnucleotide binding
D0005515molecular_functionprotein binding
D0005524molecular_functionATP binding
D0005829cellular_componentcytosol
D0006808biological_processregulation of nitrogen utilization
D0030234molecular_functionenzyme regulator activity
D0042802molecular_functionidentical protein binding
E0000166molecular_functionnucleotide binding
E0005515molecular_functionprotein binding
E0005524molecular_functionATP binding
E0005829cellular_componentcytosol
E0006808biological_processregulation of nitrogen utilization
E0030234molecular_functionenzyme regulator activity
E0042802molecular_functionidentical protein binding
F0000166molecular_functionnucleotide binding
F0005515molecular_functionprotein binding
F0005524molecular_functionATP binding
F0005829cellular_componentcytosol
F0006808biological_processregulation of nitrogen utilization
F0030234molecular_functionenzyme regulator activity
F0042802molecular_functionidentical protein binding
Functional Information from PDB Data
site_idAC1
Number of Residues20
DetailsBINDING SITE FOR RESIDUE ADP C 1109
ChainResidue
AGLY27
CPHE36
CGLY37
CARG38
CGLN39
CLYS58
CILE86
CGLY87
CASP88
CGLY89
CLYS90
AMET28
CPHE92
ATHR29
AGLU62
AVAL64
AARG101
AARG103
CILE7
CGLY35

site_idAC2
Number of Residues18
DetailsBINDING SITE FOR RESIDUE ADP D 1116
ChainResidue
DILE7
DGLY35
DPHE36
DGLY37
DARG38
DLYS58
DILE86
DGLY87
DGLY89
DLYS90
DPHE92
EGLY27
EMET28
ETHR29
EGLU62
EVAL64
EARG101
EARG103

site_idAC3
Number of Residues16
DetailsBINDING SITE FOR RESIDUE ADP E 1112
ChainResidue
EILE7
EGLY35
EPHE36
EGLY37
EARG38
ELYS58
EILE86
EGLY87
ELYS90
EPHE92
FGLY27
FMET28
FTHR29
FGLU62
FVAL64
FARG101

site_idAC4
Number of Residues18
DetailsBINDING SITE FOR RESIDUE ADP F 1115
ChainResidue
DGLY27
DMET28
DTHR29
DGLU62
DVAL64
DARG101
DARG103
FILE7
FGLY35
FPHE36
FGLY37
FARG38
FLYS58
FILE86
FGLY87
FASP88
FGLY89
FLYS90

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 B 1109
ChainResidue
AILE86
AGLY87
ALYS90
BARG101
BARG103

Functional Information from PROSITE/UniProt
site_idPS00496
Number of Residues6
DetailsPII_GLNB_UMP P-II protein uridylation site. YRGSEY
ChainResidueDetails
ATYR46-TYR51

site_idPS00638
Number of Residues14
DetailsPII_GLNB_CTER P-II protein C-terminal region signature. TgeiGDGKIFVspV
ChainResidueDetails
ATHR83-VAL96

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:7592328
ChainResidueDetails
ASER49
BSER49
CSER49
DSER49
ESER49
FSER49

site_idSWS_FT_FI2
Number of Residues6
DetailsMOD_RES: O-UMP-tyrosine => ECO:0000255|PROSITE-ProRule:PRU00675
ChainResidueDetails
ATYR51
BTYR51
CTYR51
DTYR51
ETYR51
FTYR51

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PDB entries from 2024-07-24

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