Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

1O6B

Crystal structure of phosphopantetheine adenylyltransferase with ADP

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004595molecular_functionpantetheine-phosphate adenylyltransferase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0009058biological_processbiosynthetic process
A0015937biological_processcoenzyme A biosynthetic process
A0016779molecular_functionnucleotidyltransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PO4 A 170
ChainResidue
AHIS18
AARG91
ASER128
ASER129
AADP173
AHOH226
AHOH284

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 171
ChainResidue
AHOH174
AHOH174
AHOH218
AHOH218
AASP139
AASP139

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 172
ChainResidue
ASER3
ASER3
ALYS84
ALYS84

site_idAC4
Number of Residues14
DetailsBINDING SITE FOR RESIDUE ADP A 173
ChainResidue
AGLY9
ASER10
APHE11
AGLY17
AHIS18
AILE21
AARG88
AGLY89
AARG91
AALA120
ATYR124
ALEU127
APO4170
AHOH243

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues5
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00151
ChainResidueDetails
ASER10
ALYS42
ALEU74
AARG88
AGLU99

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00151, ECO:0000305|PubMed:16021622, ECO:0007744|PDB:1O6B
ChainResidueDetails
AHIS18

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00151, ECO:0000305|PubMed:16021622
ChainResidueDetails
ATYR124

site_idSWS_FT_FI4
Number of Residues1
DetailsSITE: Transition state stabilizer => ECO:0000255|HAMAP-Rule:MF_00151
ChainResidueDetails
AHIS18

222624

PDB entries from 2024-07-17

PDB statisticsPDBj update infoContact PDBjnumon