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4OA4

CRYSTAL STRUCTURE OF A TRAP PERIPLASMIC SOLUTE BINDING PROTEIN FROM SHEWANELLA LOIHICA PV-4 (Shew_1446), TARGET EFI-510273, WITH BOUND SUCCINATE

Functional Information from GO Data
ChainGOidnamespacecontents
A0015740biological_processC4-dicarboxylate transport
A0030288cellular_componentouter membrane-bounded periplasmic space
A0042597cellular_componentperiplasmic space
A0055085biological_processtransmembrane transport
A0071702biological_processorganic substance transport
B0015740biological_processC4-dicarboxylate transport
B0030288cellular_componentouter membrane-bounded periplasmic space
B0042597cellular_componentperiplasmic space
B0055085biological_processtransmembrane transport
B0071702biological_processorganic substance transport
C0015740biological_processC4-dicarboxylate transport
C0030288cellular_componentouter membrane-bounded periplasmic space
C0042597cellular_componentperiplasmic space
C0055085biological_processtransmembrane transport
C0071702biological_processorganic substance transport
D0015740biological_processC4-dicarboxylate transport
D0030288cellular_componentouter membrane-bounded periplasmic space
D0042597cellular_componentperiplasmic space
D0055085biological_processtransmembrane transport
D0071702biological_processorganic substance transport
Functional Information from PDB Data
site_idAC1
Number of Residues12
DetailsBINDING SITE FOR RESIDUE SIN A 401
ChainResidue
AVAL41
ATYR243
AHOH504
AHOH519
AVAL42
ALYS48
ALYS101
AARG176
AMSE178
APHE199
AASN216
AASN220

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL A 402
ChainResidue
AVAL42
AALA43
AASN220
ASER223
ALYS224

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL A 403
ChainResidue
ASER75
AGLY79
AASP80
ASER200
AHOH749

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL A 404
ChainResidue
AGLN129
AGLN134
ATYR150
AHOH567
AHOH786

site_idAC5
Number of Residues12
DetailsBINDING SITE FOR RESIDUE SIN B 401
ChainResidue
BVAL41
BVAL42
BLYS48
BLYS101
BARG176
BMSE178
BPHE199
BASN216
BASN220
BTYR243
BHOH501
BHOH512

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL B 402
ChainResidue
BGLN129
BGLN134
BTYR150

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CL B 403
ChainResidue
BSER75
BGLY79
BASP80
BPHE199
BSER200
BHOH592

site_idAC8
Number of Residues12
DetailsBINDING SITE FOR RESIDUE SIN C 401
ChainResidue
CVAL41
CVAL42
CLYS48
CLYS101
CARG176
CMSE178
CPHE199
CASN216
CASN220
CTYR243
CHOH505
CHOH511

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL C 402
ChainResidue
CSER75
CASP80
CSER200
CHOH720

site_idBC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL C 403
ChainResidue
CGLN129
CGLN134
CTYR150

site_idBC2
Number of Residues12
DetailsBINDING SITE FOR RESIDUE SIN D 401
ChainResidue
DVAL41
DVAL42
DLYS48
DLYS101
DARG176
DMSE178
DPHE199
DASN216
DASN220
DTYR243
DHOH521
DHOH529

site_idBC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL D 402
ChainResidue
DSER75
DASP80
DSER200
DHOH609

site_idBC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL D 403
ChainResidue
DGLN129
DGLN134
DGLY149
DTYR150
DHOH595

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues24
DetailsBINDING: BINDING => ECO:0000269|PubMed:25540822, ECO:0007744|PDB:4OA4
ChainResidueDetails
ALYS48
ALYS101
AARG176
AASN216
AASN220
ATYR243
BLYS48
BLYS101
BARG176
BASN216
BASN220
BTYR243
CLYS48
CLYS101
CARG176
CASN216
CASN220
CTYR243
DLYS48
DLYS101
DARG176
DASN216
DASN220
DTYR243

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PDB entries from 2024-06-12

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