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6FT2

Structure of the periplasmic binding protein LAO-Q122A in complex with arginine.

Functional Information from GO Data
ChainGOidnamespacecontents
A0006865biological_processamino acid transport
A0030288cellular_componentouter membrane-bounded periplasmic space
A0042597cellular_componentperiplasmic space
A0071705biological_processnitrogen compound transport
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue EDO A 301
ChainResidue
AGLY24
APHE26
ACL305
AHOH481

site_idAC2
Number of Residues1
Detailsbinding site for residue EDO A 302
ChainResidue
AASP85

site_idAC3
Number of Residues1
Detailsbinding site for residue CL A 303
ChainResidue
ALYS44

site_idAC4
Number of Residues3
Detailsbinding site for residue CL A 304
ChainResidue
AARG93
AGLY182
AARG218

site_idAC5
Number of Residues3
Detailsbinding site for residue CL A 305
ChainResidue
APHE26
AEDO301
AHOH547

site_idAC6
Number of Residues13
Detailsbinding site for residue ARG A 306
ChainResidue
AASP11
ATYR14
APHE52
ASER69
ASER70
ASER72
AARG77
ALEU117
ASER120
ATHR121
AASP161
AHOH402
AHOH546

Functional Information from PROSITE/UniProt
site_idPS01039
Number of Residues14
DetailsSBP_BACTERIAL_3 Bacterial extracellular solute-binding proteins, family 3 signature. GFDIDLGNeMCKRM
ChainResidueDetails
AGLY28-MET41

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues7
DetailsBINDING: BINDING => ECO:0000269|PubMed:7929349, ECO:0007744|PDB:1LAH
ChainResidueDetails
AASP11
ASER69
ASER70
ASER72
AARG77
ATHR121
AASP161

224931

PDB entries from 2024-09-11

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