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3HCG

Structure of the C-terminal domain (MsrB) of Neisseria meningitidis PilB (reduced form)

Functional Information from GO Data
ChainGOidnamespacecontents
A0006979biological_processresponse to oxidative stress
A0016671molecular_functionoxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor
A0030091biological_processprotein repair
A0033743molecular_functionpeptide-methionine (R)-S-oxide reductase activity
B0006979biological_processresponse to oxidative stress
B0016671molecular_functionoxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor
B0030091biological_processprotein repair
B0033743molecular_functionpeptide-methionine (R)-S-oxide reductase activity
C0006979biological_processresponse to oxidative stress
C0016671molecular_functionoxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor
C0030091biological_processprotein repair
C0033743molecular_functionpeptide-methionine (R)-S-oxide reductase activity
D0006979biological_processresponse to oxidative stress
D0016671molecular_functionoxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor
D0030091biological_processprotein repair
D0033743molecular_functionpeptide-methionine (R)-S-oxide reductase activity
Functional Information from PDB Data
site_idAC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE PO4 A 1003
ChainResidue
AHOH33
AHOH634
CTYR462
AHOH203
AHOH360
ASER401
AASP459
AARG466
AGLU468
AHIS477
AHIS480

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PO4 B 1001
ChainResidue
AARG388
BGLU393
BGLU404
BTYR405

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PO4 D 1002
ChainResidue
BTYR462
DHOH25
DHOH136
DASP459
DARG466
DHIS477
DHIS480
DHOH565

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU01126
ChainResidueDetails
ACYS495
BCYS495
CCYS495
DCYS495

229380

PDB entries from 2024-12-25

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