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3GZG

Crystal structure of the Xanthomonas axonopodis pv. citri molybdate-binding protein (ModA) mutant (K127S)

Functional Information from GO Data
ChainGOidnamespacecontents
A0015689biological_processmolybdate ion transport
A0030288cellular_componentouter membrane-bounded periplasmic space
A0030973molecular_functionmolybdate ion binding
A0046872molecular_functionmetal ion binding
A1901359molecular_functiontungstate binding
B0015689biological_processmolybdate ion transport
B0030288cellular_componentouter membrane-bounded periplasmic space
B0030973molecular_functionmolybdate ion binding
B0046872molecular_functionmetal ion binding
B1901359molecular_functiontungstate binding
C0015689biological_processmolybdate ion transport
C0030288cellular_componentouter membrane-bounded periplasmic space
C0030973molecular_functionmolybdate ion binding
C0046872molecular_functionmetal ion binding
C1901359molecular_functiontungstate binding
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 1400
ChainResidue
AMET157
ASER160
AARG161
ALYS179
AHOH5332
AHOH5527
BARG227

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 1403
ChainResidue
AARG134
AHOH5374
AHOH5632
AHOH5841
ATHR120
AALA121

site_idAC3
Number of Residues11
DetailsBINDING SITE FOR RESIDUE MOO A 1300
ChainResidue
AALA10
AALA11
ASER12
ASER39
AALA58
AVAL123
APRO124
AALA125
ASER151
AVAL152
ATYR170

site_idAC4
Number of Residues12
DetailsBINDING SITE FOR RESIDUE MOO B 2300
ChainResidue
BALA10
BALA11
BSER12
BALA38
BSER39
BALA58
BVAL123
BPRO124
BALA125
BSER151
BVAL152
BTYR170

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 C 1402
ChainResidue
CMET157
CSER160
CARG161
CASP177
CLYS179
CARG227
CHOH5202

site_idAC6
Number of Residues12
DetailsBINDING SITE FOR RESIDUE MOO C 3300
ChainResidue
CALA10
CALA11
CSER12
CALA38
CSER39
CALA58
CVAL123
CPRO124
CALA125
CSER151
CVAL152
CTYR170

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues15
DetailsBINDING: BINDING => ECO:0000269|PubMed:16511325, ECO:0000269|PubMed:24035743, ECO:0007744|PDB:2H5Y, ECO:0007744|PDB:3GZG
ChainResidueDetails
ASER12
BTYR170
CSER12
CSER39
CALA125
CVAL152
CTYR170
ASER39
AALA125
AVAL152
ATYR170
BSER12
BSER39
BALA125
BVAL152

227344

PDB entries from 2024-11-13

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