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5MW1

cryoEM structure of crenactin double helical filament at 3.8A resolution

Replaces:  5LY4
Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0005524molecular_functionATP binding
A0005856cellular_componentcytoskeleton
A0016787molecular_functionhydrolase activity
B0000166molecular_functionnucleotide binding
B0005524molecular_functionATP binding
B0005856cellular_componentcytoskeleton
B0016787molecular_functionhydrolase activity
C0000166molecular_functionnucleotide binding
C0005524molecular_functionATP binding
C0005856cellular_componentcytoskeleton
C0016787molecular_functionhydrolase activity
D0000166molecular_functionnucleotide binding
D0005524molecular_functionATP binding
D0005856cellular_componentcytoskeleton
D0016787molecular_functionhydrolase activity
E0000166molecular_functionnucleotide binding
E0005524molecular_functionATP binding
E0005856cellular_componentcytoskeleton
E0016787molecular_functionhydrolase activity
F0000166molecular_functionnucleotide binding
F0005524molecular_functionATP binding
F0005856cellular_componentcytoskeleton
F0016787molecular_functionhydrolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues17
Detailsbinding site for residue ADP B 501
ChainResidue
BGLY19
BGLU235
BLYS238
BARG239
BGLY354
BALA355
BSER357
BTRP358
BGLN399
BTHR20
BSER21
BTYR22
BLYS24
BGLN164
BGLY183
BHIS184
BGLY185

site_idAC2
Number of Residues17
Detailsbinding site for residue ADP A 501
ChainResidue
AGLY19
ATHR20
ASER21
ATYR22
ALYS24
AGLN164
AGLY183
AHIS184
AGLY185
AGLU235
ALYS238
AARG239
AGLY354
AALA355
ASER357
ATRP358
AGLN399

site_idAC3
Number of Residues17
Detailsbinding site for residue ADP C 501
ChainResidue
CGLY19
CTHR20
CSER21
CTYR22
CLYS24
CGLN164
CGLY183
CHIS184
CGLY185
CGLU235
CLYS238
CARG239
CGLY354
CALA355
CSER357
CTRP358
CGLN399

site_idAC4
Number of Residues17
Detailsbinding site for residue ADP D 501
ChainResidue
DGLY19
DTHR20
DSER21
DTYR22
DLYS24
DGLN164
DGLY183
DHIS184
DGLY185
DGLU235
DLYS238
DARG239
DGLY354
DALA355
DSER357
DTRP358
DGLN399

site_idAC5
Number of Residues17
Detailsbinding site for residue ADP E 501
ChainResidue
EGLY19
ETHR20
ESER21
ETYR22
ELYS24
EGLN164
EGLY183
EHIS184
EGLY185
EGLU235
ELYS238
EARG239
EGLY354
EALA355
ESER357
ETRP358
EGLN399

site_idAC6
Number of Residues17
Detailsbinding site for residue ADP F 501
ChainResidue
FSER357
FTRP358
FGLN399
FGLY19
FTHR20
FSER21
FTYR22
FLYS24
FGLN164
FGLY183
FHIS184
FGLY185
FGLU235
FLYS238
FARG239
FGLY354
FALA355

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues84
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"24486010","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"24531483","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"27852434","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"27852434","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

249697

PDB entries from 2026-02-25

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