3HCG

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

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0006979	biological_process	response to oxidative stress
A	0016671	molecular_function	oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor
A	0030091	biological_process	protein repair
A	0033743	molecular_function	peptide-methionine (R)-S-oxide reductase activity
B	0006979	biological_process	response to oxidative stress
B	0016671	molecular_function	oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor
B	0030091	biological_process	protein repair
B	0033743	molecular_function	peptide-methionine (R)-S-oxide reductase activity
C	0006979	biological_process	response to oxidative stress
C	0016671	molecular_function	oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor
C	0030091	biological_process	protein repair
C	0033743	molecular_function	peptide-methionine (R)-S-oxide reductase activity
D	0006979	biological_process	response to oxidative stress
D	0016671	molecular_function	oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor
D	0030091	biological_process	protein repair
D	0033743	molecular_function	peptide-methionine (R)-S-oxide reductase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	11
Details	BINDING SITE FOR RESIDUE PO4 A 1003

Chain	Residue
A	HOH33
A	HOH634
C	TYR462
A	HOH203
A	HOH360
A	SER401
A	ASP459
A	ARG466
A	GLU468
A	HIS477
A	HIS480

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site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PO4 B 1001

Chain	Residue
A	ARG388
B	GLU393
B	GLU404
B	TYR405

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site_id	AC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE PO4 D 1002

Chain	Residue
B	TYR462
D	HOH25
D	HOH136
D	ASP459
D	ARG466
D	HIS477
D	HIS480
D	HOH565

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU01126

Chain	Residue	Details
A	CYS495
B	CYS495
C	CYS495
D	CYS495

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