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1UL3

Crystal Structure of PII from Synechocystis sp. PCC 6803

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
B0000166molecular_functionnucleotide binding
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005829cellular_componentcytosol
B0006808biological_processregulation of nitrogen utilization
B0030234molecular_functionenzyme regulator activity
C0000166molecular_functionnucleotide binding
C0005515molecular_functionprotein binding
C0005524molecular_functionATP binding
C0005829cellular_componentcytosol
C0006808biological_processregulation of nitrogen utilization
C0030234molecular_functionenzyme regulator activity
D0000166molecular_functionnucleotide binding
D0005515molecular_functionprotein binding
D0005524molecular_functionATP binding
D0005829cellular_componentcytosol
D0006808biological_processregulation of nitrogen utilization
D0030234molecular_functionenzyme regulator activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA C 601
ChainResidue
APHE11
AASP14
AGLU15
CPHE11
CASP14
CGLU15

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 602
ChainResidue
DPHE11
DASP14
DGLU15
BPHE11
BASP14
BGLU15

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 500
ChainResidue
APHE36
ALYS58
AGLY89
ALYS90
AHOH525
AHOH526
CMET28

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL C 501
ChainResidue
ALYS90
APHE92
CVAL26
CGLY27
CILE63
CVAL64
CHOH627

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. TgeiGDGKIFIspV
ChainResidueDetails
ATHR83-VAL96

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0000305
ChainResidueDetails
ASER49
BSER49
CSER49
DSER49

site_idSWS_FT_FI2
Number of Residues4
DetailsMOD_RES: O-UMP-tyrosine => ECO:0000255|PROSITE-ProRule:PRU00675
ChainResidueDetails
ATYR51
BTYR51
CTYR51
DTYR51

221051

PDB entries from 2024-06-12

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