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6F9Q

Binary complex of a 7S-cis-cis-nepetalactol cyclase from Nepeta mussinii with NAD+

Functional Information from GO Data
ChainGOidnamespacecontents
A0016099biological_processmonoterpenoid biosynthetic process
A0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A0016853molecular_functionisomerase activity
A0044283biological_processsmall molecule biosynthetic process
B0016099biological_processmonoterpenoid biosynthetic process
B0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
B0016853molecular_functionisomerase activity
B0044283biological_processsmall molecule biosynthetic process
C0016099biological_processmonoterpenoid biosynthetic process
C0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
C0016853molecular_functionisomerase activity
C0044283biological_processsmall molecule biosynthetic process
D0016099biological_processmonoterpenoid biosynthetic process
D0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
D0016853molecular_functionisomerase activity
D0044283biological_processsmall molecule biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues30
Detailsbinding site for residue NAD A 301
ChainResidue
AGLY21
AVAL71
AASN97
AALA98
AGLY99
AVAL122
AASN150
AALA151
ATYR165
ALYS169
APRO195
ASER24
AMET196
AALA197
AVAL198
ATHR200
APRO201
ALEU202
ATHR203
ACL302
AHOH411
AHOH480
AGLY25
AHOH518
AILE26
AASP46
AILE47
AGLN48
ACYS69
AASP70

site_idAC2
Number of Residues5
Detailsbinding site for residue CL A 302
ChainResidue
AGLY152
ASER153
ASER154
ATYR165
ANAD301

site_idAC3
Number of Residues31
Detailsbinding site for residue NAD B 301
ChainResidue
BGLY21
BSER24
BGLY25
BILE26
BASP46
BILE47
BGLN48
BCYS69
BASP70
BVAL71
BASN97
BALA98
BGLY99
BVAL122
BASN150
BALA151
BTYR165
BLYS169
BPRO195
BMET196
BALA197
BVAL198
BTHR200
BPRO201
BLEU202
BTHR203
BCL302
BHOH410
BHOH458
BHOH478
BHOH549

site_idAC4
Number of Residues5
Detailsbinding site for residue CL B 302
ChainResidue
BGLY152
BSER153
BSER154
BTYR165
BNAD301

site_idAC5
Number of Residues30
Detailsbinding site for residue NAD C 301
ChainResidue
CHOH510
CHOH525
CGLY21
CSER24
CGLY25
CILE26
CASP46
CILE47
CGLN48
CCYS69
CASP70
CVAL71
CASN97
CALA98
CGLY99
CASN150
CALA151
CTYR165
CLYS169
CPRO195
CMET196
CALA197
CVAL198
CTHR200
CPRO201
CLEU202
CTHR203
CCL302
CHOH408
CHOH474

site_idAC6
Number of Residues4
Detailsbinding site for residue CL C 302
ChainResidue
CGLY152
CSER153
CSER154
CNAD301

site_idAC7
Number of Residues30
Detailsbinding site for residue NAD D 301
ChainResidue
DGLY21
DSER24
DGLY25
DILE26
DASP46
DILE47
DGLN48
DCYS69
DASP70
DVAL71
DASN97
DALA98
DGLY99
DASN150
DALA151
DTYR165
DLYS169
DPRO195
DMET196
DALA197
DVAL198
DTHR200
DPRO201
DLEU202
DTHR203
DCL302
DHOH403
DHOH472
DHOH480
DHOH528

site_idAC8
Number of Residues4
Detailsbinding site for residue CL D 302
ChainResidue
DGLY152
DSER153
DSER154
DNAD301

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues24
DetailsBINDING: BINDING => ECO:0000269|PubMed:30531909, ECO:0007744|PDB:6F9Q
ChainResidueDetails
AGLY21
BASN97
BTYR165
BVAL198
CGLY21
CASP46
CASP70
CASN97
CTYR165
CVAL198
DGLY21
AASP46
DASP46
DASP70
DASN97
DTYR165
DVAL198
AASP70
AASN97
ATYR165
AVAL198
BGLY21
BASP46
BASP70

237735

PDB entries from 2025-06-18

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