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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
B0015740biological_processC4-dicarboxylate transport
B0030288cellular_componentouter membrane-bounded periplasmic space
B0042597cellular_componentperiplasmic space
B0055085biological_processtransmembrane transport
C0015740biological_processC4-dicarboxylate transport
C0030288cellular_componentouter membrane-bounded periplasmic space
C0042597cellular_componentperiplasmic space
C0055085biological_processtransmembrane transport
D0015740biological_processC4-dicarboxylate transport
D0030288cellular_componentouter membrane-bounded periplasmic space
D0042597cellular_componentperiplasmic space
D0055085biological_processtransmembrane 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
BASN216
BASN220
BTYR243
CLYS48
CLYS101
CARG176
CASN216
CASN220
CTYR243
DLYS48
ALYS101
DLYS101
DARG176
DASN216
DASN220
DTYR243
AARG176
AASN216
AASN220
ATYR243
BLYS48
BLYS101
BARG176

226707

PDB entries from 2024-10-30

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