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3OKA

Crystal structure of Corynebacterium glutamicum PimB' in complex with GDP-Man (triclinic crystal form)

Functional Information from GO Data
ChainGOidnamespacecontents
A0008654biological_processphospholipid biosynthetic process
A0009247biological_processglycolipid biosynthetic process
A0016757molecular_functionglycosyltransferase activity
A0033164molecular_functionglycolipid 1,6-alpha-mannosyltransferase activity
A0043750molecular_functionphosphatidylinositol alpha-mannosyltransferase activity
A0046488biological_processphosphatidylinositol metabolic process
A0046506biological_processsulfolipid biosynthetic process
A0046510molecular_functionUDP-sulfoquinovose:DAG sulfoquinovosyltransferase activity
B0008654biological_processphospholipid biosynthetic process
B0009247biological_processglycolipid biosynthetic process
B0016757molecular_functionglycosyltransferase activity
B0033164molecular_functionglycolipid 1,6-alpha-mannosyltransferase activity
B0043750molecular_functionphosphatidylinositol alpha-mannosyltransferase activity
B0046488biological_processphosphatidylinositol metabolic process
B0046506biological_processsulfolipid biosynthetic process
B0046510molecular_functionUDP-sulfoquinovose:DAG sulfoquinovosyltransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 601
ChainResidue
AARG206
AARG210
AARG239
AHOH387
AHOH437
DHIS-19

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 602
ChainResidue
AARG283
AHOH451
DHIS-19
ALYS54
APRO209
AARG239

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 603
ChainResidue
APRO128
AGLY129
ASER130
AARG131
AGLN132

site_idAC4
Number of Residues11
DetailsBINDING SITE FOR RESIDUE GDD A 701
ChainResidue
AARG206
AARG210
ALYS211
AVAL235
AGLY236
AARG260
ALEU261
AMET266
AGLU298
AHOH533
AHOH536

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 801
ChainResidue
ATHR71
ATHR73
AGLU360
AHOH535

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 601
ChainResidue
BARG206
BARG210
BARG239
BHOH389

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 B 602
ChainResidue
BLYS54
BARG239
BARG283

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B 603
ChainResidue
BPRO128
BGLY129
BSER130
BARG131
BGLN132

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 604
ChainResidue
BHIS50
BLYS54
CHIS-17
CHIS-18

site_idBC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE GDD B 701
ChainResidue
BARG206
BLYS211
BVAL235
BGLY236
BARG260
BLEU261
BTYR263
BMET266
BGLU298
BHOH507
BHOH510

site_idBC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 C 700
ChainResidue
CHIS-15
CHIS-14
CHIS-16

site_idBC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 D 702
ChainResidue
AHIS50
ALYS54
DHIS-17
DHIS-19
DHIS-18

site_idBC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 D 701
ChainResidue
DHIS-14
DHIS-15
DHIS-16

Functional Information from PROSITE/UniProt
site_idPS00430
Number of Residues42
DetailsTONB_DEPENDENT_REC_1 TonB-dependent receptor (TBDR) proteins signature 1. msasrktlvvtndfppriggiqsylrdfiatqdp.................................................................................ESIVVFAS
ChainResidueDetails
AMET1-SER42

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:20843801
ChainResidueDetails
AARG206
ALYS211
BLEU261
BGLU298
ALEU261
AGLU298
BARG206
BLYS211

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PDB entries from 2024-05-15

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