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4HV4

2.25 Angstrom resolution crystal structure of UDP-N-acetylmuramate--L-alanine ligase (murC) from Yersinia pestis CO92 in complex with AMP

Functional Information from GO Data
ChainGOidnamespacecontents
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0008763molecular_functionUDP-N-acetylmuramate-L-alanine ligase activity
A0009058biological_processbiosynthetic process
A0009252biological_processpeptidoglycan biosynthetic process
A0016881molecular_functionacid-amino acid ligase activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0008763molecular_functionUDP-N-acetylmuramate-L-alanine ligase activity
B0009058biological_processbiosynthetic process
B0009252biological_processpeptidoglycan biosynthetic process
B0016881molecular_functionacid-amino acid ligase activity
Functional Information from PDB Data
site_idAC1
Number of Residues18
DetailsBINDING SITE FOR RESIDUE AMP A 501
ChainResidue
AHIS128
AASP351
ATYR352
AGLY353
AGLU358
AALA361
ATHR362
AHOH662
AHOH683
AHOH706
AGLY129
ALYS130
ATHR131
ATHR132
AASN194
AHIS292
AASN296
AARG327

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE BME A 502
ChainResidue
ACYS426
AARG427

site_idAC3
Number of Residues18
DetailsBINDING SITE FOR RESIDUE AMP B 501
ChainResidue
BHIS128
BGLY129
BLYS130
BTHR131
BTHR132
BASN194
BHIS292
BASN296
BARG327
BASP351
BTYR352
BGLY353
BGLU358
BTHR362
BHOH664
BHOH701
BHOH703
BHOH727

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE BME B 502
ChainResidue
BCYS426
BARG430

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00046","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

251801

PDB entries from 2026-04-08

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