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6CVD

High resolution crystal structure of FtsY-NG domain of E. coli bound to fragment 1

Functional Information from GO Data
ChainGOidnamespacecontents
A0005525molecular_functionGTP binding
A0006614biological_processSRP-dependent cotranslational protein targeting to membrane
A0016887molecular_functionATP hydrolysis activity
B0005525molecular_functionGTP binding
B0006614biological_processSRP-dependent cotranslational protein targeting to membrane
B0016887molecular_functionATP hydrolysis activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue 4ME A 501
ChainResidue
APHE365
AASP366
AVAL403
ALYS406
AHOH651

site_idAC2
Number of Residues6
Detailsbinding site for residue 4ME A 502
ChainResidue
AGLN339
ATRP343
ATHR307
ATHR308
AGLY311
ALYS312

site_idAC3
Number of Residues6
Detailsbinding site for residue NH4 A 503
ChainResidue
ATHR331
AVAL337
AGLN354
AHIS355
ATHR356
AHOH668

site_idAC4
Number of Residues4
Detailsbinding site for residue NH4 A 504
ChainResidue
AALA328
AGLY329
AASP330
AASP382

site_idAC5
Number of Residues4
Detailsbinding site for residue 4ME B 501
ChainResidue
BTHR307
BGLY311
BGLN339
BTRP343

site_idAC6
Number of Residues5
Detailsbinding site for residue 4ME B 502
ChainResidue
BSER362
BPHE365
BASP366
BVAL403
BLYS406

site_idAC7
Number of Residues5
Detailsbinding site for residue NA B 503
ChainResidue
BASP283
BGLU284
BPHE483
BHOH646
BHOH747

Functional Information from PROSITE/UniProt
site_idPS00300
Number of Residues14
DetailsSRP54 SRP54-type proteins GTP-binding domain signature. PIrYIGVGErIedL
ChainResidueDetails
APRO467-LEU480

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00920
ChainResidueDetails
AGLY300
AASP382
ATHR446
BGLY300
BASP382
BTHR446

226707

PDB entries from 2024-10-30

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