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3RGM

Crystal structure of spin-labeled BtuB T156R1

Functional Information from GO Data
ChainGOidnamespacecontents
A0005509molecular_functioncalcium ion binding
A0005515molecular_functionprotein binding
A0006811biological_processmonoatomic ion transport
A0009279cellular_componentcell outer membrane
A0015288molecular_functionporin activity
A0015420molecular_functionABC-type vitamin B12 transporter activity
A0015889biological_processcobalamin transport
A0016020cellular_componentmembrane
A0019904molecular_functionprotein domain specific binding
A0034220biological_processmonoatomic ion transmembrane transport
A0035461biological_processvitamin transmembrane transport
A0046872molecular_functionmetal ion binding
A0046930cellular_componentpore complex
A0090482molecular_functionvitamin transmembrane transporter activity
A1902495cellular_componenttransmembrane transporter complex
Functional Information from PDB Data
site_idAC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE C8E A 800
ChainResidue
AARG358
AHOH646
AC8E805
AARG367
AGLY369
ATHR370
ATRP371
APHE470
ATHR472
AGLY473
AHOH644

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE C8E A 801
ChainResidue
ATHR338
AASP361
ASER363
ATYR383
APHE422
AHOH637
AHOH687

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE C8E A 802
ChainResidue
AILE261
AASN302
AALA313
AGLY314
ATRP431
AILE433
AALA466
AC8E804

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE C8E A 803
ChainResidue
AILE311
AGLY344
ALEU345
AGLN346
APHE353
AGLY355
AALA356
ATHR373

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE C8E A 804
ChainResidue
ATRP214
ATYR256
AILE261
ATYR436
AGLY463
AC8E802

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE C8E A 805
ChainResidue
ATRP371
ATYR505
AC8E800

site_idAC7
Number of Residues1
DetailsBINDING SITE FOR RESIDUE MG A 595
ChainResidue
ATYR256

site_idAC8
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MG A 596
ChainResidue
ATYR522
ATHR525

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG A 601
ChainResidue
AHIS174
AHIS176
AHIS449
AMG602

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG A 602
ChainResidue
AHIS174
AHIS176
AHIS449
AMG601

site_idBC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE MG A 603
ChainResidue
ASER263

site_idBC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MTN A 604
ChainResidue
ACYS156
AGLN157
ALEU168

Functional Information from PROSITE/UniProt
site_idPS01156
Number of Residues18
DetailsTONB_DEPENDENT_REC_2 TonB-dependent receptor (TBDR) proteins signature 2. YgyqTaGReYtLSGsYtF
ChainResidueDetails
ATYR577-PHE594

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues168
DetailsTOPO_DOM: Periplasmic => ECO:0000269|PubMed:12652322
ChainResidueDetails
AHIS208-THR211
AVAL306-GLY307
AGLU381-GLY382
AGLY424-GLY428
AASP471-GLY473
AGLN510-PHE514
ATYR553-LYS564
AGLN1-GLY137
AGLN159-LYS163
AGLY258
AASP350

site_idSWS_FT_FI2
Number of Residues278
DetailsTRANSMEM: Beta stranded
ChainResidueDetails
APHE197-GLU207
AASP212-ASN228
AARG243-ASN257
AGLU259-ASN276
ATHR289-ILE305
AHIS308-TRP317
ATYR333-GLY349
APHE351-ASP361
APHE365-ILE380
ATYR383-ASN397
ALYS414-GLU423
AVAL429-ASN438
ATYR453-PHE470
APRO474-ALA489
AARG497-TRP509
AASP515-ASP530
ATHR538-ALA552
AILE565-VAL576
AALA582-PHE594
ATHR138-GLY145
ATYR149-GLN158
ATHR164-THR175

site_idSWS_FT_FI3
Number of Residues106
DetailsTOPO_DOM: Extracellular => ECO:0000269|PubMed:12652322
ChainResidueDetails
ATYR229-THR242
ATYR277-ALA288
AGLN318-GLY332
AASN362-GLN364
ALEU398-GLU413
AASP439-LYS452
AILE490-LEU496
ATYR531-GLN537
ATYR577-THR581
ASER146-SER148
AHIS176-GLY196

site_idSWS_FT_FI4
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:12652322, ECO:0007744|PDB:1NQH
ChainResidueDetails
AASN72
AVAL90
AALA231
ATHR289
AARG497
ATYR531
ALEU63
ASER65

site_idSWS_FT_FI5
Number of Residues7
DetailsBINDING: BINDING => ECO:0000269|PubMed:12652322
ChainResidueDetails
ATYR229
AASP230
AASP241
AASP179
AGLN191
AASP193
AASP195

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PDB entries from 2024-06-12

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