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4FEC

Crystal Structure of Htt36Q3H

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0006974biological_processDNA damage response
A0008643biological_processcarbohydrate transport
A0015144molecular_functioncarbohydrate transmembrane transporter activity
A0015768biological_processmaltose transport
A0016020cellular_componentmembrane
A0030288cellular_componentouter membrane-bounded periplasmic space
A0034219biological_processcarbohydrate transmembrane transport
A0034289biological_processdetection of maltose stimulus
A0042597cellular_componentperiplasmic space
A0042956biological_processmaltodextrin transmembrane transport
A0043190cellular_componentATP-binding cassette (ABC) transporter complex
A0055052cellular_componentATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing
A0055085biological_processtransmembrane transport
A0060326biological_processcell chemotaxis
A0071702biological_processorganic substance transport
A1901982molecular_functionmaltose binding
A1990060cellular_componentmaltose transport complex
B0005515molecular_functionprotein binding
B0006974biological_processDNA damage response
B0008643biological_processcarbohydrate transport
B0015144molecular_functioncarbohydrate transmembrane transporter activity
B0015768biological_processmaltose transport
B0016020cellular_componentmembrane
B0030288cellular_componentouter membrane-bounded periplasmic space
B0034219biological_processcarbohydrate transmembrane transport
B0034289biological_processdetection of maltose stimulus
B0042597cellular_componentperiplasmic space
B0042956biological_processmaltodextrin transmembrane transport
B0043190cellular_componentATP-binding cassette (ABC) transporter complex
B0055052cellular_componentATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing
B0055085biological_processtransmembrane transport
B0060326biological_processcell chemotaxis
B0071702biological_processorganic substance transport
B1901982molecular_functionmaltose binding
B1990060cellular_componentmaltose transport complex
C0005515molecular_functionprotein binding
C0006974biological_processDNA damage response
C0008643biological_processcarbohydrate transport
C0015144molecular_functioncarbohydrate transmembrane transporter activity
C0015768biological_processmaltose transport
C0016020cellular_componentmembrane
C0030288cellular_componentouter membrane-bounded periplasmic space
C0034219biological_processcarbohydrate transmembrane transport
C0034289biological_processdetection of maltose stimulus
C0042597cellular_componentperiplasmic space
C0042956biological_processmaltodextrin transmembrane transport
C0043190cellular_componentATP-binding cassette (ABC) transporter complex
C0055052cellular_componentATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing
C0055085biological_processtransmembrane transport
C0060326biological_processcell chemotaxis
C0071702biological_processorganic substance transport
C1901982molecular_functionmaltose binding
C1990060cellular_componentmaltose transport complex
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ZN A 501
ChainResidue
CGLU172
CHOH644
CHOH645

site_idAC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE ZN A 502
ChainResidue
AGLU44

site_idAC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE ZN A 503
ChainResidue
AHIS39

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 504
ChainResidue
ALYS137
AHIS203
AHOH624
AHOH625

site_idAC5
Number of Residues1
DetailsBINDING SITE FOR RESIDUE ZN A 505
ChainResidue
ATYR17

site_idAC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ZN B 501
ChainResidue
BHIS203
BHOH658

site_idAC7
Number of Residues1
DetailsBINDING SITE FOR RESIDUE ZN B 502
ChainResidue
BGLU38

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ZN B 503
ChainResidue
AGLN398
BASP65
BHOH633

site_idAC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN B 504
ChainResidue
BLYS26
BGLU288
CGLU288
CZN506
CZN507

site_idBC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ZN B 505
ChainResidue
BGLU172
BZN510

site_idBC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 506
ChainResidue
AASP82
BTYR167
BLYS170
BASP180

site_idBC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 507
ChainResidue
BGLU291
CASP287
CGLU310
CZN508

site_idBC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 508
ChainResidue
BASP287
BGLU310
CGLU291
CZN508

site_idBC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ZN B 509
ChainResidue
BGLU328
BHOH603

site_idBC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 510
ChainResidue
AGLU278
BGLU172
BZN505
BHOH632

site_idBC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ZN B 511
ChainResidue
BASP82
BHOH643

site_idBC8
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ZN B 512
ChainResidue
BHOH648
BHOH649

site_idBC9
Number of Residues1
DetailsBINDING SITE FOR RESIDUE ZN C 501
ChainResidue
CLYS1

site_idCC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ZN C 502
ChainResidue
CHIS39
CHOH612

site_idCC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ZN C 503
ChainResidue
CASP95
CHOH617
CHOH618

site_idCC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ZN C 504
ChainResidue
CLYS256
CGLU328
CHOH620

site_idCC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN C 505
ChainResidue
CASP65
CMET330
CHOH621
CHOH630

site_idCC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ZN C 506
ChainResidue
BLYS26
BZN504
CZN509

site_idCC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ZN C 507
ChainResidue
BZN504
CLYS26
CZN509

site_idCC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN C 508
ChainResidue
BGLU310
BZN507
BZN508
CGLU310

site_idCC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN C 509
ChainResidue
BASP30
CLYS26
CASP30
CZN506
CZN507

site_idCC9
Number of Residues1
DetailsBINDING SITE FOR RESIDUE ZN C 510
ChainResidue
CHIS203

site_idDC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ZN C 511
ChainResidue
BHOH661
CASP209
CSER211

site_idDC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN C 512
ChainResidue
AASP207
CHIS397
CGLN400
CGLN401

site_idDC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE ZN C 513
ChainResidue
CHIS395

Functional Information from PROSITE/UniProt
site_idPS01037
Number of Residues18
DetailsSBP_BACTERIAL_1 Bacterial extracellular solute-binding proteins, family 1 signature. PIAvEalSLIYNkdlLpN
ChainResidueDetails
APRO107-ASN124

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:21685499
ChainResidueDetails
ALYS379
BLYS379
CLYS379

218853

PDB entries from 2024-04-24

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