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4W8F

Crystal structure of the dynein motor domain in the AMPPNP-bound state

Functional Information from GO Data
ChainGOidnamespacecontents
A0003796molecular_functionlysozyme activity
A0003824molecular_functioncatalytic activity
A0005524molecular_functionATP binding
A0007018biological_processmicrotubule-based movement
A0008569molecular_functionminus-end-directed microtubule motor activity
A0009253biological_processpeptidoglycan catabolic process
A0016787molecular_functionhydrolase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0016998biological_processcell wall macromolecule catabolic process
A0030286cellular_componentdynein complex
A0030430cellular_componenthost cell cytoplasm
A0031640biological_processkilling of cells of another organism
A0042742biological_processdefense response to bacterium
A0044659biological_processviral release from host cell by cytolysis
A0045505molecular_functiondynein intermediate chain binding
A0051959molecular_functiondynein light intermediate chain binding
B0003796molecular_functionlysozyme activity
B0003824molecular_functioncatalytic activity
B0005524molecular_functionATP binding
B0007018biological_processmicrotubule-based movement
B0008569molecular_functionminus-end-directed microtubule motor activity
B0009253biological_processpeptidoglycan catabolic process
B0016787molecular_functionhydrolase activity
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0016998biological_processcell wall macromolecule catabolic process
B0030286cellular_componentdynein complex
B0030430cellular_componenthost cell cytoplasm
B0031640biological_processkilling of cells of another organism
B0042742biological_processdefense response to bacterium
B0044659biological_processviral release from host cell by cytolysis
B0045505molecular_functiondynein intermediate chain binding
B0051959molecular_functiondynein light intermediate chain binding
Functional Information from PDB Data
site_idAC1
Number of Residues12
Detailsbinding site for residue ANP A 5001
ChainResidue
AILE1770
AILE1929
ALEU1970
ALYS1974
AALA1798
AGLY1799
ATHR1800
AGLY1801
ALYS1802
ATHR1803
AGLU1804
AASN1899

site_idAC2
Number of Residues17
Detailsbinding site for residue ANP A 5002
ChainResidue
ASER2048
APHE2053
AGLY2077
ACYS2078
AGLY2079
ALYS2080
ATHR2081
AALA2082
AGLU2195
AVAL2219
ACYS2220
ALYS2225
AHIS2228
AARG2507
AARG2549
AARG2552
AMG5005

site_idAC3
Number of Residues14
Detailsbinding site for residue ANP A 5003
ChainResidue
AILE2392
APRO2420
AGLY2421
AGLY2423
ALYS2424
ATHR2425
AMET2426
AGLU2488
AASN2536
AILE2570
AARG2620
ATHR2623
APRO2906
AARG2911

site_idAC4
Number of Residues12
Detailsbinding site for residue ANP A 5004
ChainResidue
AMET2732
AVAL2733
AARG2763
ATHR2764
AGLY2765
ALYS2766
ATHR2767
AILE2768
AASP2818
ACYS2892
AILE2993
AARG3512

site_idAC5
Number of Residues4
Detailsbinding site for residue MG A 5005
ChainResidue
ATHR2081
AGLU2195
AGLU2511
AANP5002

site_idAC6
Number of Residues12
Detailsbinding site for residue ANP B 5001
ChainResidue
BILE1770
BGLY1799
BGLY1801
BLYS1802
BTHR1803
BGLU1804
BASP1848
BASN1899
BILE1929
BLEU1970
BARG1971
BLYS1974

site_idAC7
Number of Residues18
Detailsbinding site for residue ANP B 5002
ChainResidue
BPHE2047
BSER2048
BPHE2053
BGLY2077
BGLY2079
BLYS2080
BTHR2081
BALA2082
BGLU2195
BVAL2219
BCYS2220
BLYS2225
BHIS2228
BARG2507
BGLU2511
BARG2549
BARG2552
BMG5005

site_idAC8
Number of Residues16
Detailsbinding site for residue ANP B 5003
ChainResidue
BILE2570
BTYR2574
BARG2620
BTHR2623
BALA2907
BARG2911
BILE2392
BPRO2420
BGLY2421
BSER2422
BGLY2423
BLYS2424
BTHR2425
BMET2426
BGLU2488
BASN2536

site_idAC9
Number of Residues12
Detailsbinding site for residue ANP B 5004
ChainResidue
BMET2732
BVAL2733
BSER2762
BARG2763
BGLY2765
BLYS2766
BTHR2767
BILE2768
BCYS2892
BTRP2920
BMET2932
BARG3512

site_idAD1
Number of Residues4
Detailsbinding site for residue MG B 5005
ChainResidue
BTHR2081
BGLU2195
BGLU2511
BANP5002

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255
ChainResidueDetails
AGLY1796
AGLY2074
AGLY2418
AGLY2760
BGLY1796
BGLY2074
BGLY2418
BGLY2760

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_04110, ECO:0000269|PubMed:3382407, ECO:0000269|PubMed:7831309, ECO:0000269|PubMed:8266098
ChainResidueDetails
AGLU3135
BGLU3135

site_idSWS_FT_FI3
Number of Residues2
DetailsACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_04110, ECO:0000269|PubMed:1892846, ECO:0000269|PubMed:3382407, ECO:0000269|PubMed:7831309, ECO:0000269|PubMed:8266098
ChainResidueDetails
AASP3144
BASP3144

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:8266098
ChainResidueDetails
ALEU3156
APHE3228
BLEU3156
BPHE3228

site_idSWS_FT_FI5
Number of Residues4
DetailsBINDING: BINDING => ECO:0000303|PubMed:7831309
ChainResidueDetails
ASER3241
AASN3256
BSER3241
BASN3256

Catalytic Information from CSA
site_idMCSA1
Number of Residues2
DetailsM-CSA 921
ChainResidueDetails
AGLU3135proton shuttle (general acid/base)
AASP3144covalent catalysis

site_idMCSA2
Number of Residues2
DetailsM-CSA 921
ChainResidueDetails
BGLU3135proton shuttle (general acid/base)
BASP3144covalent catalysis

237735

PDB entries from 2025-06-18

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