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3C8Z

The 1.6 A Crystal Structure of MshC: The Rate Limiting Enzyme in the Mycothiol Biosynthetic Pathway

Functional Information from GO Data
ChainGOidnamespacecontents
A0004817molecular_functioncysteine-tRNA ligase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0006423biological_processcysteinyl-tRNA aminoacylation
A0008270molecular_functionzinc ion binding
A0010125biological_processmycothiol biosynthetic process
A0016874molecular_functionligase activity
A0035446molecular_functioncysteine-glucosaminylinositol ligase activity
A0046872molecular_functionmetal ion binding
B0004817molecular_functioncysteine-tRNA ligase activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0006423biological_processcysteinyl-tRNA aminoacylation
B0008270molecular_functionzinc ion binding
B0010125biological_processmycothiol biosynthetic process
B0016874molecular_functionligase activity
B0035446molecular_functioncysteine-glucosaminylinositol ligase activity
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ZN A 413
ChainResidue
ACYS43
ACYS231
AHIS256

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ZN B 413
ChainResidue
BCYS43
BCYS231
BHIS256

site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SO4 B 414
ChainResidue
BLEU19
BPRO34
BHIS74
BHOH444
BHOH504
BHOH525
BHOH618
AHOH589
BARG15
BALA18

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 A 414
ChainResidue
AARG207
AARG210

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 415
ChainResidue
APRO7
AALA8
AARG119
AHOH511
AHOH569

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 B 415
ChainResidue
BPRO7
BALA8
BARG119

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 416
ChainResidue
ASER215
APRO217
AARG222
AHOH506
BHIS-1

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 417
ChainResidue
APRO353
AASP354
AGLY391
AHIS392
AASP393

site_idAC9
Number of Residues27
DetailsBINDING SITE FOR RESIDUE 5CA B 416
ChainResidue
BCYS43
BGLY44
BILE45
BTHR46
BHIS52
BGLY54
BHIS55
BTHR58
BTYR59
BASN81
BTHR83
BTRP227
BCYS231
BGLY248
BGLY249
BASP251
BLEU252
BHIS256
BGLY281
BMET282
BILE283
BHOH459
BHOH494
BHOH502
BHOH512
BHOH810
BHOH827

site_idBC1
Number of Residues22
DetailsBINDING SITE FOR RESIDUE 5CA A 418
ChainResidue
ACYS43
AGLY44
AILE45
ATHR46
AGLY54
AHIS55
ATHR58
ATYR59
AASN81
ATHR83
ATRP227
ACYS231
AGLY248
AGLY249
AASP251
ALEU252
AGLY281
AMET282
AILE283
AHOH433
AHOH479
AHOH579

site_idBC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE 1PE A 419
ChainResidue
ATYR157
AGLU209
AHOH436
AHOH477
BPRO122
BHIS124

site_idBC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE EPE B 417
ChainResidue
BTRP216
AHOH465
BMET1
BASP84
BARG101
BASP105
BTHR108
BALA128
BTHR130

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:19053270
ChainResidueDetails
ACYS43
ACYS231
AHIS256
BCYS43
BCYS231
BHIS256

site_idSWS_FT_FI2
Number of Residues10
DetailsBINDING:
ChainResidueDetails
ATHR58
BILE283
AASN81
ATRP227
AGLY249
AILE283
BTHR58
BASN81
BTRP227
BGLY249

220113

PDB entries from 2024-05-22

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