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4NAU

S. aureus CoaD with Inhibitor

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
B0003824molecular_functioncatalytic activity
B0004595molecular_functionpantetheine-phosphate adenylyltransferase activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0009058biological_processbiosynthetic process
B0015937biological_processcoenzyme A biosynthetic process
B0016779molecular_functionnucleotidyltransferase activity
C0003824molecular_functioncatalytic activity
C0004595molecular_functionpantetheine-phosphate adenylyltransferase activity
C0005524molecular_functionATP binding
C0005737cellular_componentcytoplasm
C0009058biological_processbiosynthetic process
C0015937biological_processcoenzyme A biosynthetic process
C0016779molecular_functionnucleotidyltransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues17
DetailsBINDING SITE FOR RESIDUE AGS A 201
ChainResidue
APRO9
ASER121
ATYR125
AILE128
ASER129
ASER130
ASER131
AHOH324
AHOH327
ASER11
APHE12
AGLY18
AHIS19
AILE22
AARG89
AGLY90
AARG92

site_idAC2
Number of Residues14
DetailsBINDING SITE FOR RESIDUE 2W3 A 202
ChainResidue
ALEU38
ASER41
ALYS43
APHE71
AGLY73
ALEU74
ALEU75
AARG89
ATYR99
AMET106
AASN107
AHOH312
BGLU135
BTYR139

site_idAC3
Number of Residues16
DetailsBINDING SITE FOR RESIDUE AGS B 201
ChainResidue
AARG102
BPRO9
BSER11
BPHE12
BGLY18
BHIS19
BARG89
BGLY90
BARG92
BSER121
BTYR125
BILE128
BSER129
BSER130
BSER131
BHOH310

site_idAC4
Number of Residues14
DetailsBINDING SITE FOR RESIDUE AGS C 201
ChainResidue
CSER11
CPHE12
CGLY18
CHIS19
CARG89
CGLY90
CARG92
CSER121
CTYR125
CILE128
CSER129
CSER130
CSER131
CHOH301

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00151
ChainResidueDetails
ASER11
CLYS43
CLEU75
CARG89
ALYS43
ALEU75
AARG89
BSER11
BLYS43
BLEU75
BARG89
CSER11

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00151, ECO:0000305|PubMed:24041904, ECO:0007744|PDB:4NAU
ChainResidueDetails
AHIS19
ATYR125
BHIS19
BTYR125
CHIS19
CTYR125

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00151, ECO:0000305|PubMed:24041904, ECO:0007744|PDB:4NAT, ECO:0007744|PDB:4NAU
ChainResidueDetails
AGLY90
BGLY90
CGLY90

site_idSWS_FT_FI4
Number of Residues3
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00151, ECO:0000305|PubMed:24041904, ECO:0007744|PDB:4NAH
ChainResidueDetails
AGLU100
BGLU100
CGLU100

site_idSWS_FT_FI5
Number of Residues3
DetailsBINDING: BINDING => ECO:0000305|PubMed:24041904, ECO:0007744|PDB:4NAH, ECO:0007744|PDB:4NAU
ChainResidueDetails
ASER121
BSER121
CSER121

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PDB entries from 2024-07-17

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