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3F3M

Six Crystal Structures of Two Phosphopantetheine Adenylyltransferases Reveal an Alternative Ligand Binding Mode and an Associated Structural Change

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 Residues15
DetailsBINDING SITE FOR RESIDUE PPS A 300
ChainResidue
AGLY10
ASER129
ASER130
ASER131
AHOH169
AHOH170
AHOH191
ASER11
AGLY18
AHIS19
AILE22
AARG89
AARG92
ATYR99
AILE128

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00151
ChainResidueDetails
ASER11
ALYS43
ALEU75
AARG89

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00151, ECO:0000305|PubMed:24041904, ECO:0007744|PDB:4NAU
ChainResidueDetails
AHIS19
ATYR125

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00151, ECO:0000305|PubMed:24041904, ECO:0007744|PDB:4NAT, ECO:0007744|PDB:4NAU
ChainResidueDetails
AGLY90

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00151, ECO:0000305|PubMed:24041904, ECO:0007744|PDB:4NAH
ChainResidueDetails
AGLU100

site_idSWS_FT_FI5
Number of Residues1
DetailsBINDING: BINDING => ECO:0000305|PubMed:24041904, ECO:0007744|PDB:4NAH, ECO:0007744|PDB:4NAU
ChainResidueDetails
ASER121

225946

PDB entries from 2024-10-09

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